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Conserved domains on  [gi|225436679|ref|XP_002262762|]
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protein SUPPRESSOR OF K(+) TRANSPORT GROWTH DEFECT 1 isoform X2 [Vitis vinifera]

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.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
124-294 1.80e-118

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: 342.61  E-value: 1.80e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 124 KPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 203
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 204 MGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGEsNESEASRRIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQA 283
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|.
gi 225436679 284 IRRRFDKRIYI 294
Cdd:cd19521  160 IRRRFEKRIYI 170
cell_div_CdvC super family cl49147
cell division protein CdvC;
7-429 2.39e-77

cell division protein CdvC;


The actual alignment was detected with superfamily member NF041006:

Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 244.64  E-value: 2.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLK-YEKNPkIKEAITQKFTEYLRRAEEIRavlddggagpasngd 85
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIEVLE--------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  86 aavatrpKTKPKDGEGGDGEDPEQAKLrsglnsaIIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgkrrP--W 163
Cdd:NF041006  73 -------ELVPAEPAGPDVEKESDEEL-------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgW 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 -RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESA-----PSIIFIDEIDSLCGQ 237
Cdd:NF041006 134 pRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 238 RGESNESEAsrRIKTELLVQMQGVGHNDQ--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLKARQHMFKVHLGDTph 315
Cdd:NF041006 214 YSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKI-- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 316 NLTES-DFESLAQKTEGFSGSDIavcvKDVLFEPVRKTQDAMFfintpndmwvpcgpkqpgavqismqdlaGKGLASkil 394
Cdd:NF041006 290 KLENDvDLDELAEMTEGYTASDI----RDIVQAAHMRVVKEMF----------------------------EKGLGE--- 334
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 225436679 395 PPPITKNDFDKVLARQRPTVSKSDLEVHERFTQEF 429
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 ...
124-294 1.80e-118

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: 342.61  E-value: 1.80e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 124 KPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 203
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 204 MGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGEsNESEASRRIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQA 283
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|.
gi 225436679 284 IRRRFDKRIYI 294
Cdd:cd19521  160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
60-340 1.31e-90

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 277.27  E-value: 1.31e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  60 TEYLRRAEEIRAVLDDGGAGPASNGDAAVATRPKTKPKDGEGGDGEDP--EQAKLRSGLNSAIIREKPNVKWSDVAGLES 137
Cdd:COG1222    6 TIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDAnlTQKRLGTPRGTAVPAESPDVTFDDIGGLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 215
Cdd:COG1222   86 QIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 216 QMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVgHNDQKVLVLAATNTPYALDQAIRR--RFDKRIY 293
Cdd:COG1222  165 ELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIE 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 225436679 294 IPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDI-AVC 340
Cdd:COG1222  244 VPLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLkAIV 290
cell_div_CdvC NF041006
cell division protein CdvC;
7-429 2.39e-77

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 244.64  E-value: 2.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLK-YEKNPkIKEAITQKFTEYLRRAEEIRavlddggagpasngd 85
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIEVLE--------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  86 aavatrpKTKPKDGEGGDGEDPEQAKLrsglnsaIIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgkrrP--W 163
Cdd:NF041006  73 -------ELVPAEPAGPDVEKESDEEL-------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgW 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 -RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESA-----PSIIFIDEIDSLCGQ 237
Cdd:NF041006 134 pRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 238 RGESNESEAsrRIKTELLVQMQGVGHNDQ--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLKARQHMFKVHLGDTph 315
Cdd:NF041006 214 YSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKI-- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 316 NLTES-DFESLAQKTEGFSGSDIavcvKDVLFEPVRKTQDAMFfintpndmwvpcgpkqpgavqismqdlaGKGLASkil 394
Cdd:NF041006 290 KLENDvDLDELAEMTEGYTASDI----RDIVQAAHMRVVKEMF----------------------------EKGLGE--- 334
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 225436679 395 PPPITKNDFDKVLARQRPTVSKSDLEVHERFTQEF 429
Cdd:NF041006 335 PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
120-430 2.23e-71

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: 238.65  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  120 IIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKmGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPE 522
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVGHNdQKVLVLAATNTPY 278
Cdd:TIGR01243 523 ILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQEL-SNVVVIAATNRPD 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  279 ALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDIAVCVKDVLFEPVRKTQDA 355
Cdd:TIGR01243 602 ILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679  356 mffintpndmwvPCGPKQPGAVQISMQDLAgkglaskilpppITKNDFDKVLARQRPTVSKSDLEVHERFTQEFG 430
Cdd:TIGR01243 680 ------------PAKEKLEVGEEEFLKDLK------------VEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
123-341 7.89e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 218.16  E-value: 7.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 123 EKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgkRR----PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:PRK03992 124 ESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESeASR---RIKTELLVQMQGVGHNDqKVLVLAATN 275
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDRevqRTLMQLLAEMDGFDPRG-NVKIIAATN 278
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 276 TPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTphNLTES-DFESLAQKTEGFSGSDI-AVCV 341
Cdd:PRK03992 279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLADDvDLEELAELTEGASGADLkAICT 346
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
167-296 1.56e-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: 185.10  E-value: 1.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  167 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGeSNESEA 246
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 225436679  247 SRRIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQAIRRRFDKRIYIPL 296
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
4-78 5.08e-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: 129.69  E-value: 5.08e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679   4 NFKEQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDDGGA 78
Cdd:cd02678    1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
366-430 3.39e-28

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: 105.66  E-value: 3.39e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679  366 WVPCGPKQPGAVQISMQDLAgkglASKILPPPITKNDFDKVLARQRPTVSKSDLEVHERFTQEFG 430
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-75 1.25e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.44  E-value: 1.25e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225436679     3 SNFKEQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDD 75
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLE 74
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
162-298 1.31e-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: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   162 PWRAFLLYGPPGTGKSYLAKAVATEADST---FFSVSSSDL--------------VSKWMGESEKLVSNLFQMARESAPS 224
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679   225 IIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGvghndqkVLVLAATNTPYALDQA-IRRRFDKRIYIPLPD 298
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
167-231 2.26e-04

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: 42.46  E-value: 2.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679 167 LLYGPPGTGKSYLAKAVATEA-----DSTFFSVssSDLVSKWMGE--SEKLVSNLFQMAResaPSIIFIDEI 231
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVEQLAQAraDGRLGRLLRRLAR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
124-294 1.80e-118

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: 342.61  E-value: 1.80e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 124 KPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW 203
Cdd:cd19521    1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 204 MGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGEsNESEASRRIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQA 283
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|.
gi 225436679 284 IRRRFDKRIYI 294
Cdd:cd19521  160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
60-340 1.31e-90

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 277.27  E-value: 1.31e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  60 TEYLRRAEEIRAVLDDGGAGPASNGDAAVATRPKTKPKDGEGGDGEDP--EQAKLRSGLNSAIIREKPNVKWSDVAGLES 137
Cdd:COG1222    6 TIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDAnlTQKRLGTPRGTAVPAESPDVTFDDIGGLDE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 215
Cdd:COG1222   86 QIEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 216 QMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVgHNDQKVLVLAATNTPYALDQAIRR--RFDKRIY 293
Cdd:COG1222  165 ELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF-ESRGDVLIIAATNRPDLLDPALLRpgRFDRVIE 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 225436679 294 IPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDI-AVC 340
Cdd:COG1222  244 VPLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLkAIV 290
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
132-294 5.67e-89

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: 267.30  E-value: 5.67e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 132 VAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLV 211
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 212 SNLFQMARESAPSIIFIDEIDSLCGQRGESnESEASRRIKTELLVQMQGVGHND-QKVLVLAATNTPYALDQAIRRRFDK 290
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSG-EHEASRRVKTEFLVQMDGVLNKPeDRVLVLGATNRPWELDEAFLRRFEK 159

                 ....
gi 225436679 291 RIYI 294
Cdd:cd19509  160 RIYI 163
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
131-294 3.28e-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: 245.28  E-value: 3.28e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 210
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 211 VSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVG---HNDQK---VLVLAATNTPYALDQAI 284
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGgasENDDPskmVMVLAATNFPWDIDEAL 160
                        170
                 ....*....|
gi 225436679 285 RRRFDKRIYI 294
Cdd:cd19522  161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
63-350 5.42e-78

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: 247.52  E-value: 5.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  63 LRRAEEIRAVLDDGGAGPASNGDAAVATRPKTKPKDGEGGDGEDPEQAKLRSGLNSAIIREKPNVKWSDVAGLESAKQSL 142
Cdd:COG0464   90 ELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEEL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 143 QEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARE 220
Cdd:COG0464  170 RELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 221 SAPSIIFIDEIDSLCGQRGESNESeASRRIKTELLVQMQGVGHNdqkVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLK 300
Cdd:COG0464  249 LAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEELRSD---VVVIAATNRPDLLDPALLRRFDEIIFFPLPDAE 324
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 225436679 301 ARQHMFKVHLGDTPHNlTESDFESLAQKTEGFSGSDIAVCVKDVLFEPVR 350
Cdd:COG0464  325 ERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
cell_div_CdvC NF041006
cell division protein CdvC;
7-429 2.39e-77

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 244.64  E-value: 2.39e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLK-YEKNPkIKEAITQKFTEYLRRAEEIRavlddggagpasngd 85
Cdd:NF041006   9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRlYPDSP-LRHAYEQMINEYKKRIEVLE--------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  86 aavatrpKTKPKDGEGGDGEDPEQAKLrsglnsaIIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgkrrP--W 163
Cdd:NF041006  73 -------ELVPAEPAGPDVEKESDEEL-------VVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgW 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 -RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESA-----PSIIFIDEIDSLCGQ 237
Cdd:NF041006 134 pRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 238 RGESNESEAsrRIKTELLVQMQGVGHNDQ--KVLVLAATNTPYALDQAIRRRFDKRIYIPLPDLKARQHMFKVHLGDTph 315
Cdd:NF041006 214 YSSEVGGEV--RVRNQFLKEMDGLQDKSEnyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSKI-- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 316 NLTES-DFESLAQKTEGFSGSDIavcvKDVLFEPVRKTQDAMFfintpndmwvpcgpkqpgavqismqdlaGKGLASkil 394
Cdd:NF041006 290 KLENDvDLDELAEMTEGYTASDI----RDIVQAAHMRVVKEMF----------------------------EKGLGE--- 334
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 225436679 395 PPPITKNDFDKVLARQRPTVSKSDLEVHERFTQEF 429
Cdd:NF041006 335 PRPITMEDFKEVLKIRKPSVNQEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
120-430 2.23e-71

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: 238.65  E-value: 2.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  120 IIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKmGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPE 522
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVGHNdQKVLVLAATNTPY 278
Cdd:TIGR01243 523 ILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQEL-SNVVVIAATNRPD 601
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  279 ALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDIAVCVKDVLFEPVRKTQDA 355
Cdd:TIGR01243 602 ILDPALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679  356 mffintpndmwvPCGPKQPGAVQISMQDLAgkglaskilpppITKNDFDKVLARQRPTVSKSDLEVHERFTQEFG 430
Cdd:TIGR01243 680 ------------PAKEKLEVGEEEFLKDLK------------VEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
111-294 1.85e-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: 217.93  E-value: 1.85e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 111 KLRSGLNSAIIREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADST 190
Cdd:cd19525    3 KMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGAT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 191 FFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESnESEASRRIKTELLVQMQGVG-HNDQKVL 269
Cdd:cd19525   83 FFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-EHESSRRIKTEFLVQLDGATtSSEDRIL 161
                        170       180
                 ....*....|....*....|....*
gi 225436679 270 VLAATNTPYALDQAIRRRFDKRIYI 294
Cdd:cd19525  162 VVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
131-294 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 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 210
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 211 VSNLFQMARESAPSIIFIDEIDSLCGQRgESNESEASRRIKTELLVQMQGVGHN-DQKVLVLAATNTPYALDQAIRRRFD 289
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSER-SEGEHEASRRLKTEFLIEFDGVQSNgDDRVLVMGATNRPQELDDAVLRRFT 159

                 ....*
gi 225436679 290 KRIYI 294
Cdd:cd19524  160 KRVYV 164
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
123-341 7.89e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 218.16  E-value: 7.89e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 123 EKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgkRR----PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:PRK03992 124 ESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESeASR---RIKTELLVQMQGVGHNDqKVLVLAATN 275
Cdd:PRK03992 201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDRevqRTLMQLLAEMDGFDPRG-NVKIIAATN 278
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 276 TPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTphNLTES-DFESLAQKTEGFSGSDI-AVCV 341
Cdd:PRK03992 279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--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 ...
138-294 1.13e-61

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: 197.12  E-value: 1.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLF 215
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 216 QMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVGHNDQkVLVLAATNTPYALDQAIRR--RFDKRIY 293
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIESLKG-VVVIAATNRPDMIDPALLRpgRLDKLIY 158

                 .
gi 225436679 294 I 294
Cdd:cd19511  159 V 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
123-338 5.03e-59

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 200.59  E-value: 5.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  123 EKPNVKWSDVAGLESAKQSLQEAVILpVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLV 200
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  201 SKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKT--ELLVQMQGVGHNDQkVLVLAATNTPY 278
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTlnQLLVEMDGFGTNTG-VIVIAATNRPD 204
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679  279 ALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPHNlTESDFESLAQKTEGFSGSDIA 338
Cdd:TIGR01241 205 VLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLA-PDVDLKAVARRTPGFSGADLA 265
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
167-296 1.56e-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: 185.10  E-value: 1.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  167 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGeSNESEA 246
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRG-SGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 225436679  247 SRRIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQAIRRRFDKRIYIPL 296
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
123-338 2.88e-56

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 195.26  E-value: 2.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 123 EKPNVKWSDVAGLESAKQSLQEAV-ILpvKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDL 199
Cdd:COG0465  135 DKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 200 VSkwM----GESEklVSNLFQMARESAPSIIFIDEIDSLCGQRGESN-----ESEasrriKT--ELLVQMQGVGHNDQkV 268
Cdd:COG0465  212 VE--MfvgvGASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLggghdERE-----QTlnQLLVEMDGFEGNEG-V 281
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225436679 269 LVLAATNTPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDIA 338
Cdd:COG0465  282 IVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDLEVIARRTPGFSGADLA 352
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
131-294 2.42e-55

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: 180.95  E-value: 2.42e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 208
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 209 KLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNEsEASRRIKTELLVQMQGVGhNDQKVLVLAATNTPYALDQAIRR-- 286
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQR-EVERRVVAQLLTLMDGMS-SRGKVVVIAATNRPDAIDPALRRpg 157

                 ....*...
gi 225436679 287 RFDKRIYI 294
Cdd:cd19503  158 RFDREVEI 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
131-294 2.19e-54

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: 178.39  E-value: 2.19e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFTGKR--RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 208
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 209 KLVSNLFQMARESAPSIIFIDEIDSLCGQRgESNESEASRRIKTELLVQMQGVGHNDQ-KVLVLAATNTPYALDQAIRRR 287
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDGNcRVIVMGATNRPQDLDEAILRR 159

                 ....*..
gi 225436679 288 FDKRIYI 294
Cdd:cd19520  160 MPKRFHI 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
138-294 5.57e-54

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: 177.09  E-value: 5.57e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQM 217
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225436679 218 ARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVGHNDqKVLVLAATNTPYALDQAIRR--RFDKRIYI 294
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSRS-KVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
122-351 3.36e-52

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: 186.65  E-value: 3.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  122 REKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFFtgKR---RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:TIGR01243 170 RKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELF--EHlgiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNeSEASRRIKTELLVQMQGVGHNDQkVLVLAATNTPY 278
Cdd:TIGR01243 248 IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT-GEVEKRVVAQLLTLMDGLKGRGR-VIVIGATNRPD 325
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225436679  279 ALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPhnLTES-DFESLAQKTEGFSGSDIAVCVKDVLFEPVRK 351
Cdd:TIGR01243 326 ALDPALRRpgRFDREIVIRVPDKRARKEILKVHTRNMP--LAEDvDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
121-364 1.09e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 176.11  E-value: 1.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 121 IREKPNVKWSDVAGLESAKQSLQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD 198
Cdd:PTZ00454 136 MSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 199 LVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESnESEASR---RIKTELLVQMQGVghnDQ--KVLVLAA 273
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-QTGADRevqRILLELLNQMDGF---DQttNVKVIMA 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 274 TNTPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTphNLT-ESDFESLAQKTEGFSGSDIAVCVKDVLFEPVR 350
Cdd:PTZ00454 291 TNRADTLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKM--NLSeEVDLEDFVSRPEKISAADIAAICQEAGMQAVR 368
                        250
                 ....*....|....
gi 225436679 351 KTQdamfFINTPND 364
Cdd:PTZ00454 369 KNR----YVILPKD 378
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
129-345 1.20e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 171.22  E-value: 1.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 129 WSDVAGLESAKQSLQEAVilpvkfpQFFTGKRRPwRAF--------LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLV 200
Cdd:COG1223    1 LDDVVGQEEAKKKLKLII-------KELRRRENL-RKFglwpprkiLFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 201 SKWMGESEKLVSNLFQMAREsAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVghnDQKVLVLAATNTPYAL 280
Cdd:COG1223   73 GSYLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGL---PSGSVVIAATNHPELL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679 281 DQAIRRRFDKRIYIPLPDLKARQHMFKVHLGDTPHNLtESDFESLAQKTEGFSGSDIAVCVKDVL 345
Cdd:COG1223  149 DSALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTAL 212
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
127-294 2.27e-50

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: 168.18  E-value: 2.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 127 VKWSDVAGLESAKQSLQEAVILpVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWM 204
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 205 GESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKT--ELLVQMQGVGHNDQkVLVLAATNTPYALDQ 282
Cdd:cd19501   79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTlnQLLVEMDGFESNTG-VIVIAATNRPDVLDP 157
                        170
                 ....*....|....
gi 225436679 283 AIRR--RFDKRIYI 294
Cdd:cd19501  158 ALLRpgRFDRQVYV 171
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
138-294 4.55e-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: 166.90  E-value: 4.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFTGKR-RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQ 216
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGiRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 217 MARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGVgHNDQKVLVLAATNTPYALDQAIRR--RFDKRIYI 294
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGL-EEMNGVVVIAATNRPDIIDPALLRagRFDRLIYI 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
129-292 1.48e-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: 163.28  E-value: 1.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 129 WSDVAGLESAKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGE 206
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 207 SEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEAS--RRIKTELLVQMQGVGHNDQkVLVLAATNTPYALDQAI 284
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevQRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPAL 159
                        170
                 ....*....|
gi 225436679 285 RR--RFDKRI 292
Cdd:cd19502  160 LRpgRFDRKI 169
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
131-295 7.54e-45

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: 153.36  E-value: 7.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFtgKR---RPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGES 207
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 208 EKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNeSEASRRIKTELLVQMQGVGHNDQkVLVLAATNTPYALDQAIRR- 286
Cdd:cd19519   79 ESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH-GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRf 156
                        170
                 ....*....|
gi 225436679 287 -RFDKRIYIP 295
Cdd:cd19519  157 gRFDREIDIG 166
ftsH CHL00176
cell division protein; Validated
104-338 1.10e-43

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 161.76  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 104 GEDPEQAKLRSGLNSAIIREKPN--VKWSDVAGLESAKQSLQEAVILpVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYL 179
Cdd:CHL00176 155 KGGPGQNLMNFGKSKARFQMEADtgITFRDIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLL 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 180 AKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGE-----SNESEasrRIKTEL 254
Cdd:CHL00176 233 AKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigggNDERE---QTLNQL 309
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 255 LVQMQGVGHNdQKVLVLAATNTPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPHNLtESDFESLAQKTEGF 332
Cdd:CHL00176 310 LTEMDGFKGN-KGVIVIAATNRVDILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSP-DVSLELIARRTPGF 387

                 ....*.
gi 225436679 333 SGSDIA 338
Cdd:CHL00176 388 SGADLA 393
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
125-340 2.69e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 157.24  E-value: 2.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 125 PNVKWSDVAGLESAKQSLQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSK 202
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQK 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 203 WMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEAS--RRIKTELLVQMQGV-GHNDQKVLVlaATNTPYA 279
Cdd:PTZ00361 257 YLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiQRTMLELLNQLDGFdSRGDVKVIM--ATNRIES 334
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679 280 LDQAIRR--RFDKRIYIPLPDLKARQHMFKVHlgDTPHNLTES-DFESLAQKTEGFSGSDI-AVC 340
Cdd:PTZ00361 335 LDPALIRpgRIDRKIEFPNPDEKTKRRIFEIH--TSKMTLAEDvDLEEFIMAKDELSGADIkAIC 397
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
131-294 3.14e-43

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: 149.26  E-value: 3.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKL 210
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 211 VSNLFQMARESAPSIIFIDEIDSLCGQRGEsnESEASRRIKTELLVQMQGV-GHNDQKVLVLAATNTPYALDQAIRRRFD 289
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDD--EASPVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158

                 ....*
gi 225436679 290 KRIYI 294
Cdd:cd19523  159 KRLLV 163
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
139-294 3.21e-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: 146.50  E-value: 3.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 139 KQSLQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQM 217
Cdd:cd19528    2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 218 ARESAPSIIFIDEIDSLCGQRGES--NESEASRRIKTELLVQMQGVghNDQK-VLVLAATNTPYALDQAIRR--RFDKRI 292
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNigDAGGAADRVINQILTEMDGM--NTKKnVFIIGATNRPDIIDPAILRpgRLDQLI 159

                 ..
gi 225436679 293 YI 294
Cdd:cd19528  160 YI 161
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
129-343 4.72e-42

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 157.12  E-value: 4.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 129 WSDVAGLESAKQSLQEAVIL---PVKFPQFftGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMG 205
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVG 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 206 ESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKT--ELLVQMQGVGHNdQKVLVLAATNTPYALDQA 283
Cdd:PRK10733 228 VGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTlnQMLVEMDGFEGN-EGIIVIAATNRPDVLDPA 306
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679 284 IRR--RFDKRIYIPLPDLKARQHMFKVHLGDTPHNlTESDFESLAQKTEGFSGSDIAVCVKD 343
Cdd:PRK10733 307 LLRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNE 367
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
131-292 7.53e-41

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: 142.93  E-value: 7.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFF--TGKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESE 208
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 209 KLVSNLFQMARESAPSIIFIDEIDSLCGQRgESNESEASRRIKTELLVQMQGVGHND---QKVLVLAATNTPYALDQAIR 285
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKtagGPVLVIGATNRPDSLDPALR 158

                 ....*....
gi 225436679 286 R--RFDKRI 292
Cdd:cd19518  159 RagRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
135-294 1.12e-40

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: 142.24  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 135 LESAKQSLQEAVILPVKFPQFFT--GKRRPwRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVS 212
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 213 NLFQMARESAPSIIFIDEIDSLCGQRGESnESEASRRIKTELLVQMQGvGHNDQKVLVLAATNTPYALDQAIRR--RFDK 290
Cdd:cd19530   80 QVFQRARASAPCVIFFDEVDALVPKRGDG-GSWASERVVNQLLTEMDG-LEERSNVFVIAATNRPDIIDPAMLRpgRLDK 157

                 ....
gi 225436679 291 RIYI 294
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 ...
139-294 8.46e-39

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: 137.26  E-value: 8.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 139 KQSLQEAVILPVKFPQFFTGKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMA 218
Cdd:cd19527    2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKA 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225436679 219 RESAPSIIFIDEIDSLCGQRGESNESEASR-RIKTELLVQMQGVGHNDQKVLVLAATNTPYALDQAIRR--RFDKRIYI 294
Cdd:cd19527   82 RDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLYL 160
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
4-78 5.08e-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: 129.69  E-value: 5.08e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679   4 NFKEQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDDGGA 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 ...
138-293 3.13e-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: 3.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 138 AKQSLQEAVILPVKFPQFFTGKRRPWRA-FLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGESEKLVSNLFQ 216
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSgILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225436679 217 MARESAPSIIFIDEIDSLCGQRGESNeSEASRRIKTELLVQMQGVgHNDQKVLVLAATNTPYALDQAIRR--RFDKRIY 293
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDS-TGVTDRVVNQLLTQLDGV-EGLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
131-293 4.06e-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: 128.01  E-value: 4.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQEAVILPVKFPQFFTG-KRRPWRAFLLYGPPGTGKSYLAKAVATEADS-----TFFSVSSSDLVSKWM 204
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 205 GESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRgESNESEASRRIKTELLVQMQGVGHNDQkVLVLAATNTPYALDQAI 284
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-SSKQEQIHASIVSTLLALMDGLDNRGQ-VVVIGATNRPDALDPAL 158
                        170
                 ....*....|.
gi 225436679 285 RR--RFDKRIY 293
Cdd:cd19517  159 RRpgRFDREFY 169
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
366-430 3.39e-28

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: 105.66  E-value: 3.39e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679  366 WVPCGPKQPGAVQISMQDLAgkglASKILPPPITKNDFDKVLARQRPTVSKSDLEVHERFTQEFG 430
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIP----SDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
133-296 5.57e-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: 102.61  E-value: 5.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 133 AGLESAKQSLQEAVilpvkfpqfftgKRRPWRAFLLYGPPGTGKSYLAKAVATEA---DSTFFSVSSSDLVSKWMGESEK 209
Cdd:cd00009    1 VGQEEAIEALREAL------------ELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 210 ---LVSNLFQMARESAPSIIFIDEIDSLcgqrgesneseaSRRIKTELLVQMQGV---GHNDQKVLVLAATNTPYA--LD 281
Cdd:cd00009   69 ghfLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETLndlRIDRENVRVIGATNRPLLgdLD 136
                        170
                 ....*....|....*
gi 225436679 282 QAIRRRFDKRIYIPL 296
Cdd:cd00009  137 RALYDRLDIRIVIPL 151
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
7-71 2.84e-22

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: 89.52  E-value: 2.84e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679    7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRA 71
Cdd:pfam04212   2 SKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
7-75 1.02e-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: 85.44  E-value: 1.02e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDD 75
Cdd:cd02656    4 QQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELLKK 72
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-75 1.25e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.44  E-value: 1.25e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225436679     3 SNFKEQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLDD 75
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLE 74
ycf46 CHL00195
Ycf46; Provisional
125-337 1.13e-19

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 90.85  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 125 PNVKWSDVAGLESAKQ-------SLQEAVI---LPVKfpqfftgkrrpwRAFLLYGPPGTGKSYLAKAVATEADSTFFSV 194
Cdd:CHL00195 223 VNEKISDIGGLDNLKDwlkkrstSFSKQASnygLPTP------------RGLLLVGIQGTGKSLTAKAIANDWQLPLLRL 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 195 SSSDLVSKWMGESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMqgvGHNDQKVLVLAAT 274
Cdd:CHL00195 291 DVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLATFITWL---SEKKSPVFVVATA 367
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225436679 275 NTPYALDQAIRR--RFDKRIYIPLPDLKARQHMFKVHLGDT-PHNLTESDFESLAQKTEGFSGSDI 337
Cdd:CHL00195 368 NNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSWKKYDIKKLSKLSNKFSGAEI 433
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
162-298 1.31e-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: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   162 PWRAFLLYGPPGTGKSYLAKAVATEADST---FFSVSSSDL--------------VSKWMGESEKLVSNLFQMARESAPS 224
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679   225 IIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQGvghndqkVLVLAATNTPYALDQA-IRRRFDKRIYIPLPD 298
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKN-------LTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
164-294 3.31e-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: 79.41  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVA---------TEADSTFFSVSSSDLVSKWMGESEKLVSNLFQMARE-----SAPSIIFID 229
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQEliddkDALVFVLID 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225436679 230 EIDSLCGQRGES---NESEASRRIKTELLVQMQGVGHNDQkVLVLAATNTPYALDQAIRRRFDKRIYI 294
Cdd:cd19508  133 EVESLAAARSASssgTEPSDAIRVVNAVLTQIDRIKRYHN-NVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
164-294 4.88e-17

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: 78.69  E-value: 4.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVATEADSTFFS-VSSSDLVSKWMGESEKLVSNLFQMARE--------SAPSIIFIDEIDSL 234
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESEANIRKLFADAEEeqrrlganSGLHIIIFDEIDAI 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679 235 CGQRGES-NESEASRRIKTELLVQMQGVghnDQ--KVLVLAATNTPYALDQAIRR--RFDKRIYI 294
Cdd:cd19504  116 CKQRGSMaGSTGVHDTVVNQLLSKIDGV---EQlnNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
131-294 5.60e-17

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: 77.79  E-value: 5.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 131 DVAGLESAKQSLQeavilpvKFPQFFTGKRRPW-----RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMG 205
Cdd:cd19507    1 DVGGLDNLKDWLK-------KRKAAFSKQASAYglptpKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 206 ESEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESEASRRIKTELLVQMQgvgHNDQKVLVLAATNTPYALDQAIR 285
Cdd:cd19507   74 ESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQ---EKKKPVFVVATANNVQSLPPELL 150
                        170
                 ....*....|.
gi 225436679 286 R--RFDKRIYI 294
Cdd:cd19507  151 RkgRFDEIFFV 161
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
7-73 6.32e-14

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: 66.38  E-value: 6.32e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVL 73
Cdd:cd02684    4 EKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALI 70
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
160-292 2.14e-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: 67.55  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 160 RRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSkwMG-ESEKLVSNLFQMARESAPS-IIFIDEIDSLCGQ 237
Cdd:cd19512   19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRK 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 225436679 238 RGESNESEASRRIKTELLVQMqgvGHNDQKVLVLAATNTPYALDQAIRRRFDKRI 292
Cdd:cd19512   97 RSTEKISEDLRAALNAFLYRT---GEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
153-294 2.30e-12

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: 64.68  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 153 PQFFTGKRRPW-RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSkwmgeSEKLVSNLFQMARESapSIIFIDEI 231
Cdd:cd19510   12 EDWYNDRGIPYrRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAPKQ--SIILLEDI 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 232 DS--LCGQRGESNESEA---SRRIKTELLVQMQGVGHNDQKVLVLaATNTPYALDQAIRR--RFDKRIYI 294
Cdd:cd19510   85 DAafESREHNKKNPSAYgglSRVTFSGLLNALDGVASSEERIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
164-292 7.01e-10

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: 57.54  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKWMGES--EKLVSNLFQMARESAPSIIFIDEIDSLCGQRGES 241
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 225436679 242 NESEAS-RRIKTELLVQMQGVGHNDqKVLVLAATNTPYALDQAIRRRFDKRI 292
Cdd:cd19506  107 TEKQLDpKRLKKDLPKILKSLKPED-RVLIVGTTSRPFEADLKSFCKVYNKI 157
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
7-69 2.55e-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: 53.50  E-value: 2.55e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEI 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; ...
162-294 2.50e-08

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 53.15  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 162 PWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVSKW--------------MGESEKLVSNLFQMARESAPSIIF 227
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679 228 IDEIDSLCGQRgESNESEASRRIKTELLV---QMQGVGHNDQKVLVLAATNTPYALDQAI--RRRFDKRIYI 294
Cdd:cd19505   91 IPNIHELNVNR-STQNLEEDPKLLLGLLLnylSRDFEKSSTRNILVIASTHIPQKVDPALiaPNRLDTCINI 161
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
167-295 4.04e-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: 55.24  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  167 LLYGPPGTGKSYLAKAVATE-------ADSTFFSVSSSDLVSKWMGESEKLVSNLFQMAREsapSIIFIDEIDSLCGQRG 239
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGY 392
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225436679  240 ESNESEASRRIKTeLLVQMQgvGHNDQKVLVLAAtntpYALD--------QAIRRRFDKRIYIP 295
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 ...
166-288 1.36e-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: 50.37  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  166 FLLYGPPGTGKSYLAK--AVATEADSTFF-----SVSSSDLVSKW---MGESEKLVSNLFQMARESApsIIFIDEIDslc 235
Cdd:pfam07728   2 VLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRnidPGGASWVDGPLVRAAREGE--IAVLDEIN--- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225436679  236 gqRGESNESEA-----SRRIktelLVQMQG---VGHNDQKVLVLAATNTPYA----LDQAIRRRF 288
Cdd:pfam07728  77 --RANPDVLNSllsllDERR----LLLPDGgelVKAAPDGFRLIATMNPLDRglneLSPALRSRF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
166-231 9.34e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.85  E-value: 9.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225436679 166 FLLYGPPGTGKSYLAKAVATEADSTFFSVSSS-----DLvskwmgesEKLVSNLFQMARESAPSIIFIDEI 231
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVtsgvkDL--------REVIEEARQRRSAGRRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
166-231 6.00e-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: 6.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225436679 166 FLLYGPPGTGKSYLAKAVATEADSTFFSVS--SS---DLvskwmgesEKLVSNLFQMARESAPSIIFIDEI 231
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSavTSgvkDI--------REVIEEARERRAYGRRTILFVDEI 114
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
167-234 9.81e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.43  E-value: 9.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225436679 167 LLYGPPGTGKSYLAKAVATEADSTFFSVS------SSDLVSkwmgesekLVSNLfqmareSAPSIIFIDEIDSL 234
Cdd:PRK00080  55 LLYGPPGLGKTTLANIIANEMGVNIRITSgpalekPGDLAA--------ILTNL------EEGDVLFIDEIHRL 114
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
321-356 1.36e-05

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: 42.14  E-value: 1.36e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 225436679  321 DFESLAQKTEGFSGSDIAVCVKDVLFEPVRKTQDAM 356
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
7-74 2.80e-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: 42.03  E-value: 2.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225436679   7 EQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVLD 74
Cdd:cd02683    4 LAAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIKKRLD 71
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
166-232 4.89e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 43.72  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679  166 FLLYGPPGTGKSYLAKAVA----------TEADSTFFSVSSSdlVSKWMGESEKLVS-----NLFQMARESAPSIIFIDE 230
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgderalIRIDMSEYMEEHS--VSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDE 83

                  ..
gi 225436679  231 ID 232
Cdd:pfam07724  84 IE 85
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
167-248 7.26e-05

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: 43.52  E-value: 7.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 167 LLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVskwmgESEKLVSNLFQMARESAPSIIFIDEIDSLCGqRGESNESEA 246
Cdd:cd19498   50 LMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFT-----EVGYVGRDVESIIRDLVEGIVFIDEIDKIAK-RGGSSGPDV 123

                 ..
gi 225436679 247 SR 248
Cdd:cd19498  124 SR 125
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
164-214 8.41e-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: 44.61  E-value: 8.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225436679  164 RAFLLYGPPGTGKSYLAKAVATE--ADSTFFSVSSSDLVSKWMGESEKLVSNL 214
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEALTQAF 103
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
167-200 2.22e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 42.46  E-value: 2.22e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 225436679 167 LLYGPPGTGKSYLAKAVATEA-----DSTFFSVssSDLV 200
Cdd:COG1484  103 ILLGPPGTGKTHLAIALGHEAcragyRVRFTTA--PDLV 139
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
167-231 2.26e-04

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: 42.46  E-value: 2.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679 167 LLYGPPGTGKSYLAKAVATEA-----DSTFFSVssSDLVSKWMGE--SEKLVSNLFQMAResaPSIIFIDEI 231
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAAcrqgyRVRFTTA--ADLVEQLAQAraDGRLGRLLRRLAR---YDLLIIDEL 160
PRK04195 PRK04195
replication factor C large subunit; Provisional
130-252 3.25e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.99  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 130 SDVAGLESAKQSLQEAVIlpvKFPqfftgKRRPWRAFLLYGPPGTGKSYLAKAVATEADSTFFSVSSSD-----LVSKWM 204
Cdd:PRK04195  14 SDVVGNEKAKEQLREWIE---SWL-----KGKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDqrtadVIERVA 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 225436679 205 GESEKlVSNLFQMAResapSIIFIDEIDSLCGQRGESNESEASRRIKT 252
Cdd:PRK04195  86 GEAAT-SGSLFGARR----KLILLDEVDGIHGNEDRGGARAILELIKK 128
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
164-210 7.29e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 7.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVATE--ADSTFFSVSSSDLVSKWMGESEKL 210
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFL 113
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
167-231 1.06e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 41.29  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 167 LLYGPPGTGKSYLAK----AVATEADSTFFSV------SSSDLVskwMGESEKLVSNLFQ-------------MARESAP 223
Cdd:COG1401  225 ILAGPPGTGKTYLARrlaeALGGEDNGRIEFVqfhpswSYEDFL---LGYRPSLDEGKYEptpgiflrfclkaEKNPDKP 301

                 ....*...
gi 225436679 224 SIIFIDEI 231
Cdd:COG1401  302 YVLIIDEI 309
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
167-231 1.27e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 39.41  E-value: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225436679  167 LLYGPPGTGKSYLAKAVATEADSTFFSVS------SSDLVSkwmgesekLVSNLfqmareSAPSIIFIDEI 231
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSgpaierPGDLAA--------ILTNL------EPGDVLFIDEI 93
PRK08116 PRK08116
hypothetical protein; Validated
166-186 1.44e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.39  E-value: 1.44e-03
                         10        20
                 ....*....|....*....|.
gi 225436679 166 FLLYGPPGTGKSYLAKAVATE 186
Cdd:PRK08116 117 LLLWGSVGTGKTYLAACIANE 137
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
164-231 2.65e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 39.93  E-value: 2.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVATEADST-FFSVSSSDLVSKWMGESEKLVSNLFQMARESAPsiIFIDEI 231
Cdd:COG1373   21 KAVVITGPRQVGKTTLLKQLAKELENIlYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
167-290 2.73e-03

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 40.21  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 167 LLYGPPGTGKSYLAKAVATE----------ADSTFFSVSSSDLV--SKWMGESEKLVSNLFQMARESAPSIIFIDEIDSL 234
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAWRivqgdvpevmADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225436679 235 CGQRGES-NESEASRRIKTELlvqmqgvghNDQKVLVLAAT-----NTPYALDQAIRRRFDK 290
Cdd:PRK11034 291 IGAGAASgGQVDAANLIKPLL---------SSGKIRVIGSTtyqefSNIFEKDRALARRFQK 343
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
159-232 3.02e-03

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: 38.31  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 159 KRRPWRAFLLYGPPGTGKSYLAKAVA-----TEADSTFFSVSS---SDLVSKWMGESEKLVSN-----LFQMARESAPSI 225
Cdd:cd19499   37 PNRPIGSFLFLGPTGVGKTELAKALAellfgDEDNLIRIDMSEymeKHSVSRLIGAPPGYVGYteggqLTEAVRRKPYSV 116

                 ....*..
gi 225436679 226 IFIDEID 232
Cdd:cd19499  117 VLLDEIE 123
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
167-231 3.11e-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: 38.97  E-value: 3.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225436679  167 LLYGPPGTGKSYLAKAVATEA----DSTFFsVSSSDLVSKWMGESE--KLVSNLFQMAResaPSIIFIDEI 231
Cdd:pfam01695  96 VLLGPPGVGKTHLAIALGVEAcragYSVRF-TSAADLVNQLKRAHGdgKLTRKLQQLLK---PDVLILDEW 162
PRK13341 PRK13341
AAA family ATPase;
167-231 5.00e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.27  E-value: 5.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 167 LLYGPPGTGKSYLAKAVATEADSTFFSVSS-----SDLvskwmgeSEKLVSNLFQMARESAPSIIFIDEI 231
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNAvlagvKDL-------RAEVDRAKERLERHGKRTILFIDEV 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
167-231 5.13e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.91  E-value: 5.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225436679 167 LLYGPPGTGKSYLAKAVATEADSTFFSVS------SSDLVSkwmgesekLVSNLfqmareSAPSIIFIDEI 231
Cdd:COG2255   58 LLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekPGDLAA--------ILTNL------EEGDVLFIDEI 114
44 PHA02544
clamp loader, small subunit; Provisional
140-234 6.10e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.43  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 140 QSLQEaVILPV----KFPQFFTGKRRPwrAFLLYGP-PGTGKSYLAKAVATEADSTFFSVSSSDlvskwmGESEKLVSNL 214
Cdd:PHA02544  18 STIDE-CILPAadkeTFKSIVKKGRIP--NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD------CRIDFVRNRL 88
                         90       100
                 ....*....|....*....|....
gi 225436679 215 FQ----MARESAPSIIFIDEIDSL 234
Cdd:PHA02544  89 TRfastVSLTGGGKVIIIDEFDRL 112
PRK06851 PRK06851
hypothetical protein; Provisional
164-198 6.33e-03

hypothetical protein; Provisional


Pssm-ID: 235878  Cd Length: 367  Bit Score: 38.41  E-value: 6.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 225436679 164 RAFLLYGPPGTGKSYLAKAVATEADSTFFSV----SSSD 198
Cdd:PRK06851  31 RIFILKGGPGTGKSTLMKKIGEEFLEKGYDVeflhCSSD 69
MIT_AAA_Arch cd02682
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
4-73 6.36e-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: 35.58  E-value: 6.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679   4 NFKEQAIEYVKQAVQEDNAGNYSKAFPLYMNALEYFKTHLKYEKNPKIKEAITQKFTEYLRRAEEIRAVL 73
Cdd:cd02682    1 MLEEMARKYAINAVKAEKEGNAEDAITNYKKAIEVLSQIVKNYPDSPTRLIYEQMINEYKRRIEVLEKQN 70
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
166-285 6.80e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 36.33  E-value: 6.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225436679 166 FLLYGPPGTGKSYLAKAVATEADSTFFSVSSSDLVskwmgesEKLVSNLFQMARESAPSIIFIDEIDSLCGQRGESNESE 245
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL-------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDRSSE 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 225436679 246 ASRRIKTELLVQMQG------VGHNDQKVLVLAATNTPYALDQAIR 285
Cdd:cd01120   74 LLEDLAKLLRAARNTgitviaTIHSDKFDIDRGGSSNDERLLKSLR 119
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
128-184 7.62e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 38.25  E-value: 7.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225436679 128 KWSDVAGLESAKQSLQEAVILPvKFPQfftgkrrpwrAFLLYGPPGTGKSYLAKAVA 184
Cdd:COG2812    8 TFDDVVGQEHVVRTLKNALASG-RLAH----------AYLFTGPRGVGKTTLARILA 53
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
129-185 7.63e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.51  E-value: 7.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 225436679  129 WSDVAGLESAKQSLQEAVIlpvkfpqfftGKRRpwraFLLYGPPGTGKSYLAKAVAT 185
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAA----------GGHN----LLMIGPPGSGKTMLAKRLPG 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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