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Conserved domains on  [gi|1002229220|ref|XP_015642485|]
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protein SUPPRESSOR OF K(+) TRANSPORT GROWTH DEFECT 1 isoform X2 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 103-273 1.74e-109

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19521:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 170  Bit Score: 321.43  E-value: 1.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 103 KPSVKWSDVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKW 182
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 183 MGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQA 262
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1002229220 263 MRRRFDKCIYI 273
Cdd:cd19521   160 IRRRFEKRIYI 170
cell_div_CdvC super family cl49147
cell division protein CdvC;
7-408 1.06e-70

cell division protein CdvC;


The actual alignment was detected with superfamily member NF041006:

Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 228.85  E-value: 1.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEeiraVLDGHIGGGGGGGDS 86
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRLYPDSPLRHAYEQMINEYKKRIE----VLEELVPAEPAGPDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  87 EQAKprgmLRSAIVAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFtgkrsP--W-KAFLLYGPPGTGKSYLAEAVA 163
Cdd:NF041006   85 EKES----DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 164 TEVDSTFFSISSSDLVSKWMGESEKLVANLFQMARE-----NAPSIIFIDEIDSLCGQRGecNENEASRRIKTELLVQMQ 238
Cdd:NF041006  156 NEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREkskeeGKPAIIFIDEIDALLGVYS--SEVGGEVRVRNQFLKEMD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 239 GF--DNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYIPLPDLKARKDTFKIHigdTPHSLTEG--DFVSLAYQTEGFSGS 314
Cdd:NF041006  234 GLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---TSKIKLENdvDLDELAEMTEGYTAS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 315 DIAVCVKDALFQPVRktqdaKFFIKadddtwtpsEQSQPGSIqtTMQelaskglaakillppiskiDFDEVLVRQRPTVS 394
Cdd:NF041006  311 DIRDIVQAAHMRVVK-----EMFEK---------GLGEPRPI--TME-------------------DFKEVLKIRKPSVN 355

                         410
                  ....*....|....
gi 1002229220 395 KKDLVVYEKFTQEF 408
Cdd:NF041006  356 QEMLKAYEAWHEKF 369
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 103-273 1.74e-109

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: 321.43  E-value: 1.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 103 KPSVKWSDVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKW 182
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 183 MGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQA 262
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1002229220 263 MRRRFDKCIYI 273
Cdd:cd19521   160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 40-349 1.24e-86

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.80  E-value: 1.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  40 KTHLKYEKDPKIKDAIAAKFTEYLRRAE--EIRAVLDGHIGGGGGGGDSEQAKPRGMLRSAIVAAKPSVKWSDVAGLESA 117
Cdd:COG1222     7 IDENIKALLALIDALQERLGVELALLLQpvKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 118 KEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQ 195
Cdd:COG1222    87 IEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 196 MARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQAMRR--RFDKCIYI 273
Cdd:COG1222   166 LAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEV 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 274 PLPDLKARKDTFKIHIGDTPhsLTEG-DFVSLAYQTEGFSGSDIAVCVKDAlfqpvrktqdAKFFIKADDDTWTPSE 349
Cdd:COG1222   245 PLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLKAIVTEA----------GMFAIREGRDTVTMED 309
cell_div_CdvC NF041006
cell division protein CdvC;
7-408 1.06e-70

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 228.85  E-value: 1.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEeiraVLDGHIGGGGGGGDS 86
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRLYPDSPLRHAYEQMINEYKKRIE----VLEELVPAEPAGPDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  87 EQAKprgmLRSAIVAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFtgkrsP--W-KAFLLYGPPGTGKSYLAEAVA 163
Cdd:NF041006   85 EKES----DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 164 TEVDSTFFSISSSDLVSKWMGESEKLVANLFQMARE-----NAPSIIFIDEIDSLCGQRGecNENEASRRIKTELLVQMQ 238
Cdd:NF041006  156 NEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREkskeeGKPAIIFIDEIDALLGVYS--SEVGGEVRVRNQFLKEMD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 239 GF--DNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYIPLPDLKARKDTFKIHigdTPHSLTEG--DFVSLAYQTEGFSGS 314
Cdd:NF041006  234 GLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---TSKIKLENdvDLDELAEMTEGYTAS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 315 DIAVCVKDALFQPVRktqdaKFFIKadddtwtpsEQSQPGSIqtTMQelaskglaakillppiskiDFDEVLVRQRPTVS 394
Cdd:NF041006  311 DIRDIVQAAHMRVVK-----EMFEK---------GLGEPRPI--TME-------------------DFKEVLKIRKPSVN 355

                         410
                  ....*....|....
gi 1002229220 395 KKDLVVYEKFTQEF 408
Cdd:NF041006  356 QEMLKAYEAWHEKF 369
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 104-408 4.21e-67

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 228.64  E-value: 4.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 104 PSVKWSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSK 181
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSK 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 182 WMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQ 261
Cdd:TIGR01243 527 WVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSN-VVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 262 AMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPhsLTEG-DFVSLAYQTEGFSGSDIAVCVKDALFQPVRKTqdakffi 338
Cdd:TIGR01243 606 ALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRES------- 676

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 339 kadddtwtpseqsqPGSIQTTMQELASKGLAAKILlppISKIDFDEVLVRQRPTVSKKDLVVYEKFTQEF 408
Cdd:TIGR01243 677 --------------IGSPAKEKLEVGEEEFLKDLK---VEMRHFLEALKKVKPSVSKEDMLRYERLAKEL 729
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 100-325 9.89e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 211.23  E-value: 9.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 100 VAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSD 177
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 178 LVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQR---GECNENEASRRIkTELLVQMQGFDNSnDKVLVLAATN 254
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGFDPR-GNVKIIAATN 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 255 MPHVLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTphSLTEG-DFVSLAYQTEGFSGSDI-AVCVKDALF 325
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLADDvDLEELAELTEGASGADLkAICTEAGMF 351
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 146-275 6.83e-56

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: 182.02  E-value: 6.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEA 225
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS-GGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002229220 226 SRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYIPL 275
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-74 2.24e-32

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: 118.14  E-value: 2.24e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220   4 NFKEQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLD 74
Cdd:cd02678     1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLA 71
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 345-408 1.16e-20

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: 85.24  E-value: 1.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002229220 345 WTPSEQSQPGSIQTTMQELASkglaAKILLPPISKIDFDEVLVRQRPTVSKKDLVVYEKFTQEF 408
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPS----DKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEF 60
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-77 2.23e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.05  E-value: 2.23e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220    3 SNFKEQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLDGHI 77
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 141-277 4.93e-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: 83.58  E-value: 4.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  141 PWKAFLLYGPPGTGKSYLAEAVATEVDST---FFSISSSDL--------------VSKWMGESEKLVANLFQMARENAPS 203
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220  204 IIFIDEIDSLCgqrgecnENEASRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQA-MRRRFDKCIYIPLPD 277
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 146-210 1.28e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEV----DSTFFsISSSDLVSKWMGE--SEKLVANLFQMARenaPSIIFIDEI 210
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAAcrqgYRVRF-TTAADLVEQLAQAraDGRLGRLLRRLAR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 103-273 1.74e-109

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: 321.43  E-value: 1.74e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 103 KPSVKWSDVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKW 182
Cdd:cd19521     1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 183 MGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQA 262
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGE-GESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                         170
                  ....*....|.
gi 1002229220 263 MRRRFDKCIYI 273
Cdd:cd19521   160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 40-349 1.24e-86

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 268.80  E-value: 1.24e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  40 KTHLKYEKDPKIKDAIAAKFTEYLRRAE--EIRAVLDGHIGGGGGGGDSEQAKPRGMLRSAIVAAKPSVKWSDVAGLESA 117
Cdd:COG1222     7 IDENIKALLALIDALQERLGVELALLLQpvKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 118 KEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQ 195
Cdd:COG1222    87 IEEIREAVELPLKNPELFRkyGIEPP-KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 196 MARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQAMRR--RFDKCIYI 273
Cdd:COG1222   166 LAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGFESRGD-VLIIAATNRPDLLDPALLRpgRFDRVIEV 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 274 PLPDLKARKDTFKIHIGDTPhsLTEG-DFVSLAYQTEGFSGSDIAVCVKDAlfqpvrktqdAKFFIKADDDTWTPSE 349
Cdd:COG1222   245 PLPDEEAREEILKIHLRDMP--LADDvDLDKLAKLTEGFSGADLKAIVTEA----------GMFAIREGRDTVTMED 309
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 111-273 3.52e-84

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: 256.51  E-value: 3.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 111 VAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLV 190
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 191 ANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGF-DNSNDKVLVLAATNMPHVLDQAMRRRFDK 269
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGS-GEHEASRRVKTEFLVQMDGVlNKPEDRVLVLGATNRPWELDEAFLRRFEK 159


                  ....
gi 1002229220 270 CIYI 273
Cdd:cd19509   160 RIYI 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 108-329 3.23e-74

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 239.04  E-value: 3.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 108 WSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGE 185
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKRPELREeyGLPPP-RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGE 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 186 SEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENeASRRIKTELLVQMQGFdnsNDKVLVLAATNMPHVLDQAMRR 265
Cdd:COG0464   235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLR 310

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002229220 266 RFDKCIYIPLPDLKARKDTFKIHIGDTPHSlTEGDFVSLAYQTEGFSGSDIAVCVKDALFQPVR 329
Cdd:COG0464   311 RFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 110-273 1.84e-73

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: 229.10  E-value: 1.84e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKL 189
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 190 VANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGF------DNSNDKVLVLAATNMPHVLDQAM 263
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVggasenDDPSKMVMVLAATNFPWDIDEAL 160

                         170
                  ....*....|
gi 1002229220 264 RRRFDKCIYI 273
Cdd:cd19522   161 RRRLEKRIYI 170
cell_div_CdvC NF041006
cell division protein CdvC;
7-408 1.06e-70

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 228.85  E-value: 1.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEeiraVLDGHIGGGGGGGDS 86
Cdd:NF041006    9 EMARKYAIAAVKADKEGRYEEAINNYKKAIEILTQIVRLYPDSPLRHAYEQMINEYKKRIE----VLEELVPAEPAGPDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  87 EQAKprgmLRSAIVAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFtgkrsP--W-KAFLLYGPPGTGKSYLAEAVA 163
Cdd:NF041006   85 EKES----DEELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-----PlgWpRGILLYGPPGCGKTMLAAAVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 164 TEVDSTFFSISSSDLVSKWMGESEKLVANLFQMARE-----NAPSIIFIDEIDSLCGQRGecNENEASRRIKTELLVQMQ 238
Cdd:NF041006  156 NEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREkskeeGKPAIIFIDEIDALLGVYS--SEVGGEVRVRNQFLKEMD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 239 GF--DNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYIPLPDLKARKDTFKIHigdTPHSLTEG--DFVSLAYQTEGFSGS 314
Cdd:NF041006  234 GLqdKSENYHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYY---TSKIKLENdvDLDELAEMTEGYTAS 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 315 DIAVCVKDALFQPVRktqdaKFFIKadddtwtpsEQSQPGSIqtTMQelaskglaakillppiskiDFDEVLVRQRPTVS 394
Cdd:NF041006  311 DIRDIVQAAHMRVVK-----EMFEK---------GLGEPRPI--TME-------------------DFKEVLKIRKPSVN 355

                         410
                  ....*....|....
gi 1002229220 395 KKDLVVYEKFTQEF 408
Cdd:NF041006  356 QEMLKAYEAWHEKF 369
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 94-273 3.40e-68

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: 216.01  E-value: 3.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  94 MLRSAIVAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSI 173
Cdd:cd19525     7 LIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 174 SSSDLVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGFDNS-NDKVLVLAA 252
Cdd:cd19525    87 SASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGE-GEHESSRRIKTEFLVQLDGATTSsEDRILVVGA 165

                         170       180
                  ....*....|....*....|.
gi 1002229220 253 TNMPHVLDQAMRRRFDKCIYI 273
Cdd:cd19525   166 TNRPQEIDEAARRRLVKRLYI 186
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 104-408 4.21e-67

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 228.64  E-value: 4.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 104 PSVKWSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSK 181
Cdd:TIGR01243 448 PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSK 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 182 WMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQ 261
Cdd:TIGR01243 527 WVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDRIVNQLLTEMDGIQELSN-VVVIAATNRPDILDP 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 262 AMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPhsLTEG-DFVSLAYQTEGFSGSDIAVCVKDALFQPVRKTqdakffi 338
Cdd:TIGR01243 606 ALLRpgRFDRLILVPPPDEEARKEIFKIHTRSMP--LAEDvDLEELAEMTEGYTGADIEAVCREAAMAALRES------- 676

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 339 kadddtwtpseqsqPGSIQTTMQELASKGLAAKILlppISKIDFDEVLVRQRPTVSKKDLVVYEKFTQEF 408
Cdd:TIGR01243 677 --------------IGSPAKEKLEVGEEEFLKDLK---VEMRHFLEALKKVKPSVSKEDMLRYERLAKEL 729
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 110-273 4.65e-64

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: 204.70  E-value: 4.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKL 189
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 190 VANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGF-DNSNDKVLVLAATNMPHVLDQAMRRRFD 268
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSE-GEHEASRRLKTEFLIEFDGVqSNGDDRVLVMGATNRPQELDDAVLRRFT 159


                  ....*
gi 1002229220 269 KCIYI 273
Cdd:cd19524   160 KRVYV 164
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 100-325 9.89e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 211.23  E-value: 9.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 100 VAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSD 177
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIEPP-KGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 178 LVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQR---GECNENEASRRIkTELLVQMQGFDNSnDKVLVLAATN 254
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTL-MQLLAEMDGFDPR-GNVKIIAATN 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 255 MPHVLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTphSLTEG-DFVSLAYQTEGFSGSDI-AVCVKDALF 325
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHTRKM--NLADDvDLEELAELTEGASGADLkAICTEAGMF 351
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 102-334 3.65e-58

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: 199.43  E-value: 3.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 102 AKPSVKWSDVAGLESAKEALQEAAILpIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLV 179
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFV 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 180 SKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKT--ELLVQMQGFDnSNDKVLVLAATNMPH 257
Cdd:TIGR01241 126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTlnQLLVEMDGFG-TNTGVIVIAATNRPD 204

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 258 VLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPHSlTEGDFVSLAYQTEGFSGSDIAVCVKDALFQPVRKTQDA 334
Cdd:TIGR01241 205 VLDPALLRpgRFDRQVVVDLPDIKGREEILKVHAKNKKLA-PDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTE 282
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 146-275 6.83e-56

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: 182.02  E-value: 6.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGEcNENEA 225
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS-GGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002229220 226 SRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYIPL 275
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 117-273 9.80e-55

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: 180.17  E-value: 9.80e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 117 AKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLF 194
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 195 QMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDnSNDKVLVLAATNMPHVLDQAMRR--RFDKCIY 272
Cdd:cd19511    80 QKARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELDGIE-SLKGVVVIAATNRPDMIDPALLRpgRLDKLIY 158


                  .
gi 1002229220 273 I 273
Cdd:cd19511   159 V 159
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
99-317 3.02e-54

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 191.02  E-value: 3.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  99 IVAAKPSVKWSDVAGLESAKEALQEaailpI----KFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFS 172
Cdd:COG0465   132 YDEDKPKVTFDDVAGVDEAKEELQE-----IvdflKDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 173 ISSSDLVSkwM----GESEklVANLFQMARENAPSIIFIDEIDSLCGQRG--------EcneneasrRIKT--ELLVQMQ 238
Cdd:COG0465   206 ISGSDFVE--MfvgvGASR--VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdE--------REQTlnQLLVEMD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 239 GFDnSNDKVLVLAATNMPHVLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPhsLTEG-DFVSLAYQTEGFSGSD 315
Cdd:COG0465   274 GFE-GNEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVHARKKP--LAPDvDLEVIARRTPGFSGAD 350


                  ..
gi 1002229220 316 IA 317
Cdd:COG0465   351 LA 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 ...
 110-273 5.00e-53

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 175.94  E-value: 5.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESE 187
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRalGLKPP-RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 188 KLVANLFQMARENAPSIIFIDEIDSLCGQRGECNEnEASRRIKTELLVQMQGFDNSNdKVLVLAATNMPHVLDQAMRR-- 265
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQR-EVERRVVAQLLTLMDGMSSRG-KVVVIAATNRPDAIDPALRRpg 157


                  ....*...
gi 1002229220 266 RFDKCIYI 273
Cdd:cd19503   158 RFDREVEI 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 110-273 7.80e-52

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: 172.99  E-value: 7.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFTGKR--SPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESE 187
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 188 KLVANLFQMARENAPSIIFIDEIDSLCGQRgECNENEASRRIKTELLVQMQGFDNS-NDKVLVLAATNMPHVLDQAMRRR 266
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR-SSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAILRR 159


                  ....*..
gi 1002229220 267 FDKCIYI 273
Cdd:cd19520   160 MPKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 104-432 5.45e-51

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 184.73  E-value: 5.45e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 104 PSVKWSDVAGLESAKEALQEAAILPIKFPHFFtgKR---SPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVS 180
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELF--EHlgiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMS 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 181 KWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNeNEASRRIKTELLVQMQGFdNSNDKVLVLAATNMPHVLD 260
Cdd:TIGR01243 251 KYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVT-GEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALD 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 261 QAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPHSlTEGDFVSLAYQTEGFSGSDIAVCVKDALFQPVRK-TQDAKFF 337
Cdd:TIGR01243 329 PALRRpgRFDREIVIRVPDKRARKEILKVHTRNMPLA-EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfIREGKIN 407

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 338 IKADDdtwTPSEQSQpgSIQTTMQELASkglAAKILLPPISKidfdEVLVrQRPTVSKKDLVVYEKFTQEFSEeeifisp 417
Cdd:TIGR01243 408 FEAEE---IPAEVLK--ELKVTMKDFME---ALKMVEPSAIR----EVLV-EVPNVRWSDIGGLEEVKQELRE------- 467

                         330
                  ....*....|....*
gi 1002229220 418 lSNEKPQSHDVPFKK 432
Cdd:TIGR01243 468 -AVEWPLKHPEIFEK 481
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 106-273 5.79e-51

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: 170.88  E-value: 5.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 106 VKWSDVAGLESAKEALQEAaILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWM 183
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEV-VEFLKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 184 GESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKT--ELLVQMQGFDnSNDKVLVLAATNMPHVLDQ 261
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTlnQLLVEMDGFE-SNTGVIVIAATNRPDVLDP 157

                         170
                  ....*....|....
gi 1002229220 262 AMRR--RFDKCIYI 273
Cdd:cd19501   158 ALLRpgRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 108-271 2.47e-50

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: 169.06  E-value: 2.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 108 WSDVAGLESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGE 185
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEelGIEPP-KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 186 SEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECN---ENEAsRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQA 262
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGtggDREV-QRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPA 158

                         170
                  ....*....|.
gi 1002229220 263 MRR--RFDKCI 271
Cdd:cd19502   159 LLRpgRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 117-273 6.06e-50

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 167.46  E-value: 6.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 117 AKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQM 196
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 197 ARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFdNSNDKVLVLAATNMPHVLDQAMRR--RFDKCIYI 273
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGV-NSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 117-273 5.98e-48

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: 162.28  E-value: 5.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 117 AKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLF 194
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKrlGIRPP-KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 195 QMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQAMRR--RFDKCIY 272
Cdd:cd19529    80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELDGLEEMNG-VVVIAATNRPDIIDPALLRagRFDRLIY 158


                  .
gi 1002229220 273 I 273
Cdd:cd19529   159 I 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 103-330 8.47e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 166.86  E-value: 8.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 103 KPSVKWSDVAGLESAKEALQEAAILPIKFPHFF--TGKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVS 180
Cdd:PTZ00454  139 KPDVTYSDIGGLDIQKQEIREAVELPLTCPELYeqIGIDPP-RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 181 KWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECnENEASR---RIKTELLVQMQGFDNSNDkVLVLAATNMPH 257
Cdd:PTZ00454  218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDA-QTGADRevqRILLELLNQMDGFDQTTN-VKVIMATNRAD 295

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 258 VLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPHSlTEGDFVSLAYQTEGFSGSDIAVCVKDALFQPVRK 330
Cdd:PTZ00454  296 TLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMNLS-EEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
108-324 3.49e-46

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 160.82  E-value: 3.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 108 WSDVAGLESAKEALQE------AAILPIKFphfftgKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSK 181
Cdd:COG1223     1 LDDVVGQEEAKKKLKLiikelrRRENLRKF------GLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 182 WMGESEKLVANLFQMAREnAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMqgfDNSNDKVLVLAATNMPHVLDQ 261
Cdd:COG1223    75 YLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQEL---DGLPSGSVVIAATNHPELLDS 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002229220 262 AMRRRFDKCIYIPLPDLKARKDTFKIHIGDTPHSLTEgDFVSLAYQTEGFSGSDIAVCVKDAL 324
Cdd:COG1223   151 ALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPFEL-DLKKLAKKLEGLSGADIEKVLKTAL 212
ftsH CHL00176
cell division protein; Validated
 102-331 1.10e-44

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 165.61  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 102 AKPSVKWSDVAGLESAKEALQEAAILpIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLV 179
Cdd:CHL00176  176 ADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFV 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 180 SKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGE--CNENEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPH 257
Cdd:CHL00176  254 EMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiGGGNDEREQTLNQLLTEMDGFKGNKG-VIVIAATNRVD 332

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 258 VLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIGDTPhsltEGDFVSL---AYQTEGFSGSDIAVCVKDALFQPVRKT 331
Cdd:CHL00176  333 ILDAALLRpgRFDRQITVSLPDREGRLDILKVHARNKK----LSPDVSLeliARRTPGFSGADLANLLNEAAILTARRK 407
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 100-324 1.36e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 159.17  E-value: 1.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 100 VAAKPSVKWSDVAGLESAKEALQEAAILPIKFPHFF--TGKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSD 177
Cdd:PTZ00361  174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIKPP-KGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 178 LVSKWMGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECN---ENEASRRIkTELLVQMQGFDNSNDkVLVLAATN 254
Cdd:PTZ00361  253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATsggEKEIQRTM-LELLNQLDGFDSRGD-VKVIMATN 330

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002229220 255 MPHVLDQAMRR--RFDKCIYIPLPDLKARKDTFKIHIgdTPHSLTEG-DFVSLAYQTEGFSGSDI-AVCVKDAL 324
Cdd:PTZ00361  331 RIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHT--SKMTLAEDvDLEEFIMAKDELSGADIkAICTEAGL 402
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 110-274 3.30e-43

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 150.28  E-value: 3.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFtgKR---SPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGES 186
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELF--KAigiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 187 EKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNeNEASRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQAMRR- 265
Cdd:cd19519    79 ESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTH-GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRf 156

                         170
                  ....*....|
gi 1002229220 266 -RFDKCIYIP 274
Cdd:cd19519   157 gRFDREIDIG 166
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
108-323 3.85e-42

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 158.66  E-value: 3.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 108 WSDVAGLESAKEALQEAaILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGE 185
Cdd:PRK10733  151 FADVAGCDEAKEEVAEL-VEYLREPSRFQklGGKIP-KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 186 SEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKT--ELLVQMQGFDnSNDKVLVLAATNMPHVLDQAM 263
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTlnQMLVEMDGFE-GNEGIIVIAATNRPDVLDPAL 307

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002229220 264 RR--RFDKCIYIPLPDLKARKDTFKIHIGDTPHSlTEGDFVSLAYQTEGFSGSDIAVCVKDA 323
Cdd:PRK10733  308 LRpgRFDRQVVVGLPDVRGREQILKVHMRRVPLA-PDIDAAIIARGTPGFSGADLANLVNEA 368
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 118-273 3.54e-41

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 144.58  E-value: 3.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 118 KEALQEAAILPIKFPHFFTG-KRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQM 196
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 197 ARENAPSIIFIDEIDSLCGQRG--ECNENEASRRIKTELLVQMQGFdNSNDKVLVLAATNMPHVLDQAMRR--RFDKCIY 272
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGgnIGDAGGAADRVINQILTEMDGM-NTKKNVFIIGATNRPDIIDPAILRpgRLDQLIY 160


                  .
gi 1002229220 273 I 273
Cdd:cd19528   161 I 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 114-273 1.07e-39

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 140.70  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 114 LESAKEALQEAAILPIKFPHFFT--GKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVA 191
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 192 NLFQMARENAPSIIFIDEIDSLCGQRGEcNENEASRRIKTELLVQMQGFDNSNdKVLVLAATNMPHVLDQAMRR--RFDK 269
Cdd:cd19530    80 QVFQRARASAPCVIFFDEVDALVPKRGD-GGSWASERVVNQLLTEMDGLEERS-NVFVIAATNRPDIIDPAMLRpgRLDK 157


                  ....
gi 1002229220 270 CIYI 273
Cdd:cd19530   158 TLYV 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 110-271 1.79e-39

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 140.23  E-value: 1.79e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFF--TGKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESE 187
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVEPP-RGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 188 KLVANLFQMARENAPSIIFIDEIDSLCGQRgECNENEASRRIKTELLVQMQGFDNSNDK---VLVLAATNMPHVLDQAMR 264
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKR-ESAQREMERRIVSQLLTCMDELNNEKTAggpVLVIGATNRPDSLDPALR 158


                  ....*....
gi 1002229220 265 R--RFDKCI 271
Cdd:cd19518   159 RagRFDREI 167
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 110-273 7.45e-39

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: 138.48  E-value: 7.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFTGKRSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKL 189
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 190 VANLFQMARENAPSIIFIDEIDSLCGQRGEcnENEASRRIKTELLVQMQGFDNS-NDKVLVLAATNMPHVLDQAMRRRFD 268
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQDD--EASPVGRLQVELLAQLDGVLGSgEDGVLVVCTTSKPEEIDESLRRYFS 158


                  ....*
gi 1002229220 269 KCIYI 273
Cdd:cd19523   159 KRLLV 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 118-273 2.52e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 134.18  E-value: 2.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 118 KEALQEAAILPIKFPHFFT---GKRSpwkAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLF 194
Cdd:cd19527     2 KKEILDTIQLPLEHPELFSsglRKRS---GILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 195 QMARENAPSIIFIDEIDSLCGQRGECNENEASR-RIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQAMRR--RFDKCI 271
Cdd:cd19527    79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMdRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLL 158


                  ..
gi 1002229220 272 YI 273
Cdd:cd19527   159 YL 160
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 117-272 1.24e-34

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: 127.16  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 117 AKEALQEAAILPIKFPHFFTGKRSPWKA-FLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESEKLVANLFQ 195
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRSgILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 196 MARENAPSIIFIDEIDSLCGQRGECNENeASRRIKTELLVQMQGFDnSNDKVLVLAATNMPHVLDQAMRR--RFDKCIY 272
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTG-VTDRVVNQLLTQLDGVE-GLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 110-272 1.65e-33

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: 124.54  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQEAAILPIKFPHFFTG-KRSPWKAFLLYGPPGTGKSYLAEAVATEVDS-----TFFSISSSDLVSKWM 183
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 184 GESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTeLLVQMQGFDNSNdKVLVLAATNMPHVLDQAM 263
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVST-LLALMDGLDNRG-QVVVIGATNRPDALDPAL 158

                         170
                  ....*....|.
gi 1002229220 264 RR--RFDKCIY 272
Cdd:cd19517   159 RRpgRFDREFY 169
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-74 2.24e-32

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: 118.14  E-value: 2.24e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220   4 NFKEQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLD 74
Cdd:cd02678     1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLA 71
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 112-275 1.00e-23

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: 96.83  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 112 AGLESAKEALQEAAILPikfphfftgkrsPWKAFLLYGPPGTGKSYLAEAVATEV---DSTFFSISSSDLVSKWMGESEK 188
Cdd:cd00009     1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 189 ---LVANLFQMARENAPSIIFIDEIDSLcgqrgecneneaSRRIKTELLVQMQGFDN---SNDKVLVLAATN--MPHVLD 260
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL------------SRGAQNALLRVLETLNDlriDRENVRVIGATNrpLLGDLD 136

                         170
                  ....*....|....*
gi 1002229220 261 QAMRRRFDKCIYIPL 275
Cdd:cd00009   137 RALYDRLDIRIVIPL 151
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 345-408 1.16e-20

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: 85.24  E-value: 1.16e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002229220 345 WTPSEQSQPGSIQTTMQELASkglaAKILLPPISKIDFDEVLVRQRPTVSKKDLVVYEKFTQEF 408
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPS----DKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEF 60
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
3-77 2.23e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 85.05  E-value: 2.23e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220    3 SNFKEQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLDGHI 77
Cdd:smart00745   2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 7-71 1.19e-19

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: 82.59  E-value: 1.19e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRA 71
Cdd:pfam04212   2 SKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 141-277 4.93e-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: 83.58  E-value: 4.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  141 PWKAFLLYGPPGTGKSYLAEAVATEVDST---FFSISSSDL--------------VSKWMGESEKLVANLFQMARENAPS 203
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220  204 IIFIDEIDSLCgqrgecnENEASRRIKTELLVQMQGFDNSNDKVLVLAATNMPHVLDQA-MRRRFDKCIYIPLPD 277
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 7-74 1.52e-18

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: 79.66  E-value: 1.52e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLD 74
Cdd:cd02656     4 QQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELLK 71
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 143-265 1.30e-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: 80.23  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEVDSTFFSI-SSSDLVSKWMGESEKLVANLFQMARENAPS--------IIFIDEIDSL 213
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002229220 214 CGQRGECNENEA-SRRIKTELLVQMQGFDNSNDkVLVLAATNMPHVLDQAMRR 265
Cdd:cd19504   116 CKQRGSMAGSTGvHDTVVNQLLSKIDGVEQLNN-ILVIGMTNRKDLIDEALLR 167
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 110-273 9.62e-16

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 74.71  E-value: 9.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 110 DVAGLESAKEALQ--EAAILPikfPHFFTGKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGESE 187
Cdd:cd19507     1 DVGGLDNLKDWLKkrKAAFSK---QASAYGLPTP-KGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 188 KLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQgfdNSNDKVLVLAATNMPHVLDQAMRR-- 265
Cdd:cd19507    77 SRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSGTSSRVLGTFLTWLQ---EKKKPVFVVATANNVQSLPPELLRkg 153


                  ....*...
gi 1002229220 266 RFDKCIYI 273
Cdd:cd19507   154 RFDEIFFV 161
ycf46 CHL00195
Ycf46; Provisional
 104-316 1.77e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 78.52  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 104 PSVKWSDVAGLESAKEAL-QEAAILPIKFPHFftGKRSPwKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKW 182
Cdd:CHL00195  223 VNEKISDIGGLDNLKDWLkKRSTSFSKQASNY--GLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 183 MGESEKLVANLFQMARENAPSIIFIDEIDSLCGQRGECNENEASRRIKTELLVQMQgfdNSNDKVLVLAATNMPHVLDQA 262
Cdd:CHL00195  300 VGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVLATFITWLS---EKKSPVFVVATANNIDLLPLE 376

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 263 MRR--RFDKCIYIPLPDLKARKDTFKIHIGDT-PHSLTEGDFVSLAYQTEGFSGSDI 316
Cdd:CHL00195  377 ILRkgRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSWKKYDIKKLSKLSNKFSGAEI 433
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 143-273 6.06e-15

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: 73.25  E-value: 6.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEVD---------STFFSISSSDLVSKWMGESEKLVANLFQMARE-----NAPSIIFID 208
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFQKIQEliddkDALVFVLID 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002229220 209 EIDSLCGQRGEC---NENEASRRIKTELLVQMQGFdNSNDKVLVLAATNMPHVLDQAMRRRFDKCIYI 273
Cdd:cd19508   133 EVESLAAARSASssgTEPSDAIRVVNAVLTQIDRI-KRYHNNVILLTSNLLEKIDVAFVDRADIKQYI 199
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-73 7.04e-13

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


Pssm-ID: 239147  Cd Length: 75  Bit Score: 63.68  E-value: 7.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVL 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 ...
 139-271 1.46e-10

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 59.46  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 139 RSPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSkwMG-ESEKLVANLFQMA-RENAPSIIFIDEIDSLCGQ 216
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRK 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 217 RGECNENEASRRIKTELLVQMQgfDNSNDKVLVLaATNMPHVLDQAMRRRFDKCI 271
Cdd:cd19512    97 RSTEKISEDLRAALNAFLYRTG--EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 143-273 1.73e-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: 59.46  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKWMGES--EKLVANLFQMARENAPSIIFIDEIDSLCGQRGEC 220
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 221 NENEAS-RRIKTELLVQMQGFdNSNDKVLVLAATNMPHVLD-QAMRRRFDKCIYI 273
Cdd:cd19506   107 TEKQLDpKRLKKDLPKILKSL-KPEDRVLIVGTTSRPFEADlKSFCKVYNKIILI 160
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 140-273 2.44e-10

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 58.93  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 140 SPWKAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSKW--------------MGESEKLVANLFQMARENAPSII 205
Cdd:cd19505    10 SPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCII 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002229220 206 FIDEIDSLCGQRgECNENEASRRIKTELLVQMQGFDNSND---KVLVLAATNMPHVLDQAM--RRRFDKCIYI 273
Cdd:cd19505    90 WIPNIHELNVNR-STQNLEEDPKLLLGLLLNYLSRDFEKSstrNILVIASTHIPQKVDPALiaPNRLDTCINI 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 129-273 1.42e-09

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 56.59  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 129 IKFPHFFTGKRSPWK-AFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVSkwmgeSEKLVANLFQMARENapSIIFI 207
Cdd:cd19510     9 IKNEDWYNDRGIPYRrGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAPKQ--SIILL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 208 DEID-SLCGQRGECNENEASRRIKTellVQMQGFDNSNDKV------LVLAATNMPHVLDQAMRR--RFDKCIYI 273
Cdd:cd19510    82 EDIDaAFESREHNKKNPSAYGGLSR---VTFSGLLNALDGVasseerIVFMTTNHIERLDPALIRpgRVDMKIYM 153
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 145-210 9.30e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.94  E-value: 9.30e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 145 FLLYGPPGTGKSYLAEAVATEVDSTFFSISSS-----DLvskwmgesEKLVANLFQMARENAPSIIFIDEI 210
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVtsgvkDL--------REVIEEARQRRSAGRRTILFIDEI 101
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 146-274 3.11e-07

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: 52.92  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEV-------DSTFFSISSSDLVSKWMGESEKLVANLFQMAREnapSIIFIDEIDSLCgQRG 218
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIYcglgvlrKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLV-ETG 391

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 219 ECNENEASRRIKTELLVQMQgfdNSNDKVLVLAA---TNMPHVLD--QAMRRRFDKCIYIP 274
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARME---NDRDRLVVIGAgyrKDLDKFLEvnEGLRSRFTRVIEFP 449
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 7-69 3.16e-07

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: 47.73  E-value: 3.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEI 69
Cdd:cd02677     4 EQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDSSPERREAVKRKIAEYLKRAEEI 66
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 145-210 4.79e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.98  E-value: 4.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 145 FLLYGPPGTGKSYLAEAVATEVDSTFFSIS--SS---DLvskwmgesEKLVANLFQMARENAPSIIFIDEI 210
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSavTSgvkDI--------REVIEEARERRAYGRRTILFVDEI 114
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 145-267 2.29e-06

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 46.90  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 145 FLLYGPPGTGKSYLAE--AVATEVDSTFF-----SISSSDLVSKW---MGESEKLVANLFQMAREnaPSIIFIDEIDslc 214
Cdd:pfam07728   2 VLLVGPPGTGKTELAErlAAALSNRPVFYvqltrDTTEEDLFGRRnidPGGASWVDGPLVRAARE--GEIAVLDEIN--- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002229220 215 gqrgECNENEAS--------RRIKTELLVQMQGFDnsNDKVLVLAATNMP----HVLDQAMRRRF 267
Cdd:pfam07728  77 ----RANPDVLNsllslldeRRLLLPDGGELVKAA--PDGFRLIATMNPLdrglNELSPALRSRF 135
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
146-213 8.53e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.82  E-value: 8.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSIS------SSDLVSkwmgesekLVANLfqmaRENapSIIFIDEIDSL 213
Cdd:PRK00080   55 LLYGPPGLGKTTLANIIANEMGVNIRITSgpalekPGDLAA--------ILTNL----EEG--DVLFIDEIHRL 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
 109-165 1.38e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.61  E-value: 1.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 109 SDVAGLESAKEALQEAAIlpiKFPHfftgkRSPWKAFLLYGPPGTGKSYLAEAVATE 165
Cdd:PRK04195   14 SDVVGNEKAKEQLREWIE---SWLK-----GKPKKALLLYGPPGVGKTSLAHALAND 62
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 300-334 4.25e-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: 40.60  E-value: 4.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1002229220 300 DFVSLAYQTEGFSGSDIAVCVKDALFQPVRKTQDA 334
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 7-75 5.78e-05

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


Pssm-ID: 239146  Cd Length: 77  Bit Score: 41.26  E-value: 5.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220   7 EQAIEYVKQAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLDG 75
Cdd:cd02683     4 LAAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIKKRLDQ 72
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 108-164 7.18e-05

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: 43.68  E-value: 7.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 108 WSDVAGLESAKEALQEAAIlpikfphfftGKRSpwkaFLLYGPPGTGKSYLAEAVAT 164
Cdd:pfam01078   2 LADVKGQEQAKRALEIAAA----------GGHN----LLMIGPPGSGKTMLAKRLPG 44
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 145-211 8.63e-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: 42.95  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 145 FLLYGPPGTGKSYLAEAVA----------TEVDSTFFSISSSdlVSKWMGESEKLVA-----NLFQMARENAPSIIFIDE 209
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellfgderalIRIDMSEYMEEHS--VSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDE 83


                  ..
gi 1002229220 210 ID 211
Cdd:pfam07724  84 IE 85
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 143-193 1.41e-04

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: 43.84  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEV--DSTFFSISSSDLVSKWMGESEKLVANL 193
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTEALTQAF 103
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 146-293 3.11e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 43.29  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEV----------DSTFFSISSSDLV--SKWMGESEKLVANLFQMARENAPSIIFIDEIDSL 213
Cdd:PRK11034  211 LLVGESGVGKTAIAEGLAWRIvqgdvpevmaDCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 214 CGQ-RGECNENEASRRIKTELlvqmqgfdnSNDKVLVLAATNMPHV-----LDQAMRRRFDKcIYIPLPDLkarKDTFKI 287
Cdd:PRK11034  291 IGAgAASGGQVDAANLIKPLL---------SSGKIRVIGSTTYQEFsnifeKDRALARRFQK-IDITEPSI---EETVQI 357


                  ....*.
gi 1002229220 288 HIGDTP 293
Cdd:PRK11034  358 INGLKP 363
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
143-189 3.93e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 42.65  E-value: 3.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEV--DSTFFSISSSDLVSKWMGESEKL 189
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTEFL 113
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 143-227 5.34e-04

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 40.83  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLVskwmgESEKLVANLFQMARENAPSIIFIDEIDSLCGqRGECNE 222
Cdd:cd19498    47 KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFT-----EVGYVGRDVESIIRDLVEGIVFIDEIDKIAK-RGGSSG 120


                  ....*
gi 1002229220 223 NEASR 227
Cdd:cd19498   121 PDVSR 125
PRK08116 PRK08116
hypothetical protein; Validated
 145-235 6.28e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.54  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 145 FLLYGPPGTGKSYLAEAVATEVdstffsisssdlvskwmgeSEKLVANLFQmareNAPSIifIDEIDSLCGQRGECNENE 224
Cdd:PRK08116  117 LLLWGSVGTGKTYLAACIANEL-------------------IEKGVPVIFV----NFPQL--LNRIKSTYKSSGKEDENE 171

                          90
                  ....*....|..
gi 1002229220 225 ASRRIK-TELLV 235
Cdd:PRK08116  172 IIRSLVnADLLI 183
PRK13341 PRK13341
AAA family ATPase;
146-210 8.60e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 41.96  E-value: 8.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSISS-----SDLvskwmgeSEKLVANLFQMARENAPSIIFIDEI 210
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNAvlagvKDL-------RAEVDRAKERLERHGKRTILFIDEV 118
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 146-210 1.28e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEV----DSTFFsISSSDLVSKWMGE--SEKLVANLFQMARenaPSIIFIDEI 210
Cdd:NF038214   94 LLLGPPGTGKTHLAIALGYAAcrqgYRVRF-TTAADLVEQLAQAraDGRLGRLLRRLAR---YDLLIIDEL 160
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 15-267 1.69e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  15 QAVQEDNGGNYVKAFPLYMNALEYFKTHLKYEKDPKIKDAIAAKFTEYLRRAEEIRAVLDGHIGGGGGGGDSEQAKPRGM 94
Cdd:COG1401    97 AAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220  95 LRSAIVAAKPSVKWSDVAGLESAKEALQEAAILPIKfpHFFTGKRSPwKAFLLYGPPGTGKSYL----AEAVATEVDSTF 170
Cdd:COG1401   177 LAAELSAAEELYSEDLESEDDYLKDLLREKFEETLE--AFLAALKTK-KNVILAGPPGTGKTYLarrlAEALGGEDNGRI 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002229220 171 FSI------SSSDLVskwMGESEKLVANLFQ-----------MAREN--APSIIFIDEIdslcgqrgecneNEA------ 225
Cdd:COG1401   254 EFVqfhpswSYEDFL---LGYRPSLDEGKYEptpgiflrfclKAEKNpdKPYVLIIDEI------------NRAnvekyf 318

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 226 --------SRRIKTELLVQMQGFDNSN-----DKVLVLAATNMPH----VLDQAMRRRF 267
Cdd:COG1401   319 gellslleSDKRGEELSIELPYSGEGEefsipPNLYIIGTMNTDDrslaLSDKALRRRF 377
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
107-163 2.74e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 39.79  E-value: 2.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002229220 107 KWSDVAGLESAKEALQeAAILPIKFPHfftgkrspwkAFLLYGPPGTGKSYLAEAVA 163
Cdd:COG2812     8 TFDDVVGQEHVVRTLK-NALASGRLAH----------AYLFTGPRGVGKTTLARILA 53
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
146-165 3.61e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.99  E-value: 3.61e-03
                          10        20
                  ....*....|....*....|
gi 1002229220 146 LLYGPPGTGKSYLAEAVATE 165
Cdd:COG1484   103 ILLGPPGTGKTHLAIALGHE 122
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 146-210 4.22e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 39.29  E-value: 4.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSIS------SSDLVSkwmgesekLVANLfqmaRENapSIIFIDEI 210
Cdd:COG2255    58 LLYGPPGLGKTTLAHIIANEMGVNIRITSgpaiekPGDLAA--------ILTNL----EEG--DVLFIDEI 114
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 146-210 4.68e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 37.86  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSIS------SSDLVSkwmgesekLVANLfqmareNAPSIIFIDEI 210
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSgpaierPGDLAA--------ILTNL------EPGDVLFIDEI 93
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 110-174 5.29e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 37.92  E-value: 5.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002229220 110 DVAGLESAKEALQEaailpikfpHFFTGKRSP---WKAFLLYGPPGTGKSYLAEAVATEVDSTFFSIS 174
Cdd:cd19500    11 DHYGLEDVKERILE---------YLAVRKLKGsmkGPILCLVGPPGVGKTSLGKSIARALGRKFVRIS 69
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 146-211 8.64e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 37.96  E-value: 8.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002229220 146 LLYGPPGTGKSYLAEAVATEVDSTFFSISSSDLV-SKWMGES-EKLVANLFQMARENAPS----IIFIDEID 211
Cdd:cd19497    54 LLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLLQAADYDVERaqrgIVYIDEID 125
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
143-210 9.03e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 38.39  E-value: 9.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002229220 143 KAFLLYGPPGTGKSYLAEAVATEVDST-FFSISSSDLVSKWMGESEKLVANLFQMARENAPsiIFIDEI 210
Cdd:COG1373    21 KAVVITGPRQVGKTTLLKQLAKELENIlYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
 
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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