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Conserved domains on  [gi|1983106055|gb|KAG2991641|]
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Spastin [Phytophthora cactorum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 139-301 5.38e-98

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: 289.25  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 139 IAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLV 218
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 219 RALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRLEKR 298
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 1983106055 299 IYV 301
Cdd:cd19509   161 IYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 52-395 7.48e-91

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


:

Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 277.27  E-value: 7.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  52 NEEAKTHMRHKINEYMLRAEYLKDWMAEQARKQQTQNASVSSTHEGNARTESGRQQQRAGYSkqhaehahtILDEVLDHS 131
Cdd:COG1222     2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTP---------RGTAVPAES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 132 PGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSK 209
Cdd:COG1222    73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 210 WVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRS-ASENEASRRIKNQFFTELDGAASSqeDRILVMGATNLPQELD 288
Cdd:COG1222   152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLAELDGFESR--GDVLIIAATNRPDLLD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 289 EAIIR--RLEKRIYVPLPDASSREGLIRHLLSSQKfTLSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRelgakvanv 366
Cdd:COG1222   230 PALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIR--------- 299

                         330       340
                  ....*....|....*....|....*....
gi 1983106055 367 kaEDVRGINASDFQVALTRVRPSVSSTTI 395
Cdd:COG1222   300 --EGRDTVTMEDLEKAIEKVKKKTETATN 326
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 10-75 2.95e-11

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: 58.71  E-value: 2.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983106055  10 EDAIQKtIEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKD 75
Cdd:pfam04212   2 SKALEL-VKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 139-301 5.38e-98

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: 289.25  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 139 IAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLV 218
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 219 RALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRLEKR 298
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 1983106055 299 IYV 301
Cdd:cd19509   161 IYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 52-395 7.48e-91

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 277.27  E-value: 7.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  52 NEEAKTHMRHKINEYMLRAEYLKDWMAEQARKQQTQNASVSSTHEGNARTESGRQQQRAGYSkqhaehahtILDEVLDHS 131
Cdd:COG1222     2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTP---------RGTAVPAES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 132 PGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSK 209
Cdd:COG1222    73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 210 WVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRS-ASENEASRRIKNQFFTELDGAASSqeDRILVMGATNLPQELD 288
Cdd:COG1222   152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLAELDGFESR--GDVLIIAATNRPDLLD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 289 EAIIR--RLEKRIYVPLPDASSREGLIRHLLSSQKfTLSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRelgakvanv 366
Cdd:COG1222   230 PALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIR--------- 299

                         330       340
                  ....*....|....*....|....*....
gi 1983106055 367 kaEDVRGINASDFQVALTRVRPSVSSTTI 395
Cdd:COG1222   300 --EGRDTVTMEDLEKAIEKVKKKTETATN 326
cell_div_CdvC NF041006
cell division protein CdvC;
10-405 2.85e-88

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 271.99  E-value: 2.85e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  10 EDAIQKTIEEAVAVDKAGKYAEAVELYASGIEkMMTQMAQL-PNEEAKTHMRHKINEYMLRAEYLKdwmaEQARKQQTQN 88
Cdd:NF041006    8 EEMARKYAIAAVKADKEGRYEEAINNYKKAIE-ILTQIVRLyPDSPLRHAYEQMINEYKKRIEVLE----ELVPAEPAGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  89 ASVSSTHEgnartesgrqqqragyskqhaehahtilDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFtglra 168
Cdd:NF041006   83 DVEKESDE----------------------------ELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF----- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 169 P---PRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEMAREL-----QPSVVFMDEIDA 240
Cdd:NF041006  130 PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKskeegKPAIIFIDEIDA 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 241 LLSTRSaSENEASRRIKNQFFTELDGAASSQED-RILVMGATNLPQELDEAIIRRLEKRIYVPLPDASSREGLIRHLLSS 319
Cdd:NF041006  210 LLGVYS-SEVGGEVRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSK 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 320 QKFTlSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRELGAKvanvKAEDVRGINASDFQVALTRVRPSVSSTTIQDLV 399
Cdd:NF041006  289 IKLE-NDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK----GLGEPRPITMEDFKEVLKIRKPSVNQEMLKAYE 363


                  ....*.
gi 1983106055 400 AWNEQY 405
Cdd:NF041006  364 AWHEKF 369
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 124-387 4.05e-72

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: 231.34  E-value: 4.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 124 LDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNI 201
Cdd:COG0464   144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLP-PPRGLLLYGPPGTGKTLLARALAGELGLPLIEV 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 202 SASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGaassQEDRILVMGAT 281
Cdd:COG0464   223 DLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE----LRSDVVVIAAT 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 282 NLPQELDEAIIRRLEKRIYVPLPDASSREGLIRHLLSSQKFTlSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRELGA 361
Cdd:COG0464   299 NRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377

                         250       260
                  ....*....|....*....|....*.
gi 1983106055 362 KvanvkaedvrgINASDFQVALTRVR 387
Cdd:COG0464   378 P-----------VTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 128-387 8.94e-70

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 225.10  E-value: 8.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 128 LDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASS 205
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIE-PPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 206 LTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASR---RIKNQFFTELDGAASSQEDRIlvMGATN 282
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGFDPRGNVKI--IAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 283 LPQELDEAIIR--RLEKRIYVPLPDASSREGLIR-HllsSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGPIRe 358
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKiH---TRKMNLADDvDLEELAELTEGASGADLKAICTEAGMFAIR- 354

                         250       260
                  ....*....|....*....|....*....
gi 1983106055 359 lgakvanvkaEDVRGINASDFQVALTRVR 387
Cdd:PRK03992  355 ----------DDRTEVTMEDFLKAIEKVM 373
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 122-406 4.16e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 229.02  E-value: 4.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 122 TILDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFF 199
Cdd:TIGR01243 438 SAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLAKAVATESGANFI 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 200 NISASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEA-SRRIKNQFFTELDGAASSQEdrILVM 278
Cdd:TIGR01243 517 AVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSN--VVVI 594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 279 GATNLPQELDEAIIR--RLEKRIYVPLPDASSREGLIRhlLSSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGP 355
Cdd:TIGR01243 595 AATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLAEDvDLEELAEMTEGYTGADIEAVCREAAMAA 672

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055 356 IRELGAKVANVKAEDVRG-------INASDFQVALTRVRPSVSSTTIQDLVAWNEQYG 406
Cdd:TIGR01243 673 LRESIGSPAKEKLEVGEEeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 173-303 1.97e-58

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: 187.03  E-value: 1.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEA 252
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1983106055 253 SRRIKNQFFTELDGaASSQEDRILVMGATNLPQELDEAIIRRLEKRIYVPL 303
Cdd:pfam00004  81 SRRVVNQLLTELDG-FTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 169-305 6.91e-20

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 6.91e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  169 PPRGVLLFGPPGTGKTLLAKAVATEAKAT---FFNISASSLTS--------------KWVGEGEKLVRALFEMARELQPS 231
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983106055  232 VVFMDEIDALLSTRSASENEASRRIKNQFFTEldgaassQEDRILVMGATNLPQELDEAIIR-RLEKRIYVPLPD 305
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 10-75 2.95e-11

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: 58.71  E-value: 2.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983106055  10 EDAIQKtIEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKD 75
Cdd:pfam04212   2 SKALEL-VKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 11-82 2.96e-10

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: 56.12  E-value: 2.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983106055  11 DAIQKTIEE---AVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKDWMAEQAR 82
Cdd:cd02678     1 DFLQKAIELvkkAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 328-363 2.74e-07

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: 46.76  E-value: 2.74e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1983106055 328 EFKHIVKATEGYSGSDLKAVCKDAALGPIRELGAKV 363
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
17-74 2.45e-06

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 44.99  E-value: 2.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055   17 IEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLK 74
Cdd:smart00745  12 ISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIK 69
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 173-194 2.30e-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: 39.38  E-value: 2.30e-03
                          10        20
                  ....*....|....*....|..
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEA 194
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAA 114
 
Name Accession Description Interval E-value
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 139-301 5.38e-98

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: 289.25  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 139 IAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLV 218
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 219 RALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRLEKR 298
Cdd:cd19509    81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                  ...
gi 1983106055 299 IYV 301
Cdd:cd19509   161 IYI 163
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 123-301 9.25e-95

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: 282.26  E-value: 9.25e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 123 ILDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNIS 202
Cdd:cd19525     8 IMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSIS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 203 ASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATN 282
Cdd:cd19525    88 ASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATN 167

                         170
                  ....*....|....*....
gi 1983106055 283 LPQELDEAIIRRLEKRIYV 301
Cdd:cd19525   168 RPQEIDEAARRRLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 138-301 3.22e-93

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: 277.12  E-value: 3.22e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKL 217
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 218 VRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRLEK 297
Cdd:cd19524    81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                  ....
gi 1983106055 298 RIYV 301
Cdd:cd19524   161 RVYV 164
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 52-395 7.48e-91

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 277.27  E-value: 7.48e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  52 NEEAKTHMRHKINEYMLRAEYLKDWMAEQARKQQTQNASVSSTHEGNARTESGRQQQRAGYSkqhaehahtILDEVLDHS 131
Cdd:COG1222     2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTP---------RGTAVPAES 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 132 PGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSK 209
Cdd:COG1222    73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGIE-PPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 210 WVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRS-ASENEASRRIKNQFFTELDGAASSqeDRILVMGATNLPQELD 288
Cdd:COG1222   152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLAELDGFESR--GDVLIIAATNRPDLLD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 289 EAIIR--RLEKRIYVPLPDASSREGLIRHLLSSQKfTLSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRelgakvanv 366
Cdd:COG1222   230 PALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIR--------- 299

                         330       340
                  ....*....|....*....|....*....
gi 1983106055 367 kaEDVRGINASDFQVALTRVRPSVSSTTI 395
Cdd:COG1222   300 --EGRDTVTMEDLEKAIEKVKKKTETATN 326
cell_div_CdvC NF041006
cell division protein CdvC;
10-405 2.85e-88

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 271.99  E-value: 2.85e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  10 EDAIQKTIEEAVAVDKAGKYAEAVELYASGIEkMMTQMAQL-PNEEAKTHMRHKINEYMLRAEYLKdwmaEQARKQQTQN 88
Cdd:NF041006    8 EEMARKYAIAAVKADKEGRYEEAINNYKKAIE-ILTQIVRLyPDSPLRHAYEQMINEYKKRIEVLE----ELVPAEPAGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  89 ASVSSTHEgnartesgrqqqragyskqhaehahtilDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFtglra 168
Cdd:NF041006   83 DVEKESDE----------------------------ELVVKEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF----- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 169 P---PRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEMAREL-----QPSVVFMDEIDA 240
Cdd:NF041006  130 PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKskeegKPAIIFIDEIDA 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 241 LLSTRSaSENEASRRIKNQFFTELDGAASSQED-RILVMGATNLPQELDEAIIRRLEKRIYVPLPDASSREGLIRHLLSS 319
Cdd:NF041006  210 LLGVYS-SEVGGEVRVRNQFLKEMDGLQDKSENyHVYVIGATNKPWRLDEPFLRRFQKRIYIPLPDREQRLELLKYYTSK 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 320 QKFTlSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRELGAKvanvKAEDVRGINASDFQVALTRVRPSVSSTTIQDLV 399
Cdd:NF041006  289 IKLE-NDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK----GLGEPRPITMEDFKEVLKIRKPSVNQEMLKAYE 363


                  ....*.
gi 1983106055 400 AWNEQY 405
Cdd:NF041006  364 AWHEKF 369
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 132-301 4.01e-79

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: 241.69  E-value: 4.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 132 PGVHWTDIAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWV 211
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 212 GEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSqEDRILVMGATNLPQELDEAI 291
Cdd:cd19521    82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGND-SQGVLVLGATNIPWQLDSAI 160

                         170
                  ....*....|
gi 1983106055 292 IRRLEKRIYV 301
Cdd:cd19521   161 RRRFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 138-301 8.84e-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: 225.25  E-value: 8.84e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKL 217
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 218 VRALFEMARELQPSVVFMDEIDALLSTR-SASENEASRRIKNQFFTELDGAASSQEDR-----ILVMGATNLPQELDEAI 291
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                         170
                  ....*....|
gi 1983106055 292 IRRLEKRIYV 301
Cdd:cd19522   161 RRRLEKRIYI 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 124-387 4.05e-72

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: 231.34  E-value: 4.05e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 124 LDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNI 201
Cdd:COG0464   144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREeyGLP-PPRGLLLYGPPGTGKTLLARALAGELGLPLIEV 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 202 SASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGaassQEDRILVMGAT 281
Cdd:COG0464   223 DLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE----LRSDVVVIAAT 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 282 NLPQELDEAIIRRLEKRIYVPLPDASSREGLIRHLLSSQKFTlSSREFKHIVKATEGYSGSDLKAVCKDAALGPIRELGA 361
Cdd:COG0464   299 NRPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRPLD-EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377

                         250       260
                  ....*....|....*....|....*.
gi 1983106055 362 KvanvkaedvrgINASDFQVALTRVR 387
Cdd:COG0464   378 P-----------VTTEDLLEALERED 392
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 138-301 1.35e-71

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: 221.91  E-value: 1.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLF--TGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGE 215
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFdnSRLLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 216 KLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRL 295
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                  ....*.
gi 1983106055 296 EKRIYV 301
Cdd:cd19520   161 PKRFHI 166
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 128-387 8.94e-70

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 225.10  E-value: 8.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 128 LDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASS 205
Cdd:PRK03992  122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEevGIE-PPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 206 LTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASR---RIKNQFFTELDGAASSQEDRIlvMGATN 282
Cdd:PRK03992  201 LVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDRevqRTLMQLLAEMDGFDPRGNVKI--IAATN 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 283 LPQELDEAIIR--RLEKRIYVPLPDASSREGLIR-HllsSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGPIRe 358
Cdd:PRK03992  279 RIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKiH---TRKMNLADDvDLEELAELTEGASGADLKAICTEAGMFAIR- 354

                         250       260
                  ....*....|....*....|....*....
gi 1983106055 359 lgakvanvkaEDVRGINASDFQVALTRVR 387
Cdd:PRK03992  355 ----------DDRTEVTMEDFLKAIEKVM 373
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 122-406 4.16e-68

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 229.02  E-value: 4.16e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 122 TILDEVLDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFF 199
Cdd:TIGR01243 438 SAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIR-PPKGVLLFGPPGTGKTLLAKAVATESGANFI 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 200 NISASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEA-SRRIKNQFFTELDGAASSQEdrILVM 278
Cdd:TIGR01243 517 AVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSN--VVVI 594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 279 GATNLPQELDEAIIR--RLEKRIYVPLPDASSREGLIRhlLSSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGP 355
Cdd:TIGR01243 595 AATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIFK--IHTRSMPLAEDvDLEELAEMTEGYTGADIEAVCREAAMAA 672

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055 356 IRELGAKVANVKAEDVRG-------INASDFQVALTRVRPSVSSTTIQDLVAWNEQYG 406
Cdd:TIGR01243 673 LRESIGSPAKEKLEVGEEeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 173-303 1.97e-58

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: 187.03  E-value: 1.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEA 252
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1983106055 253 SRRIKNQFFTELDGaASSQEDRILVMGATNLPQELDEAIIRRLEKRIYVPL 303
Cdd:pfam00004  81 SRRVVNQLLTELDG-FTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 145-301 3.68e-58

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: 187.10  E-value: 3.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 145 AKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEM 224
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 225 ARELQPSVVFMDEIDALLSTRSAS-ENEASRRIKNQFFTELDGAASsqEDRILVMGATNLPQELDEAIIR--RLEKRIYV 301
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNS--RSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 145-301 2.65e-57

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: 185.18  E-value: 2.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 145 AKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALF 222
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKrlGIR-PPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 223 EMARELQPSVVFMDEIDALLSTRSAS-ENEASRRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR--RLEKRI 299
Cdd:cd19511    80 QKARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                  ..
gi 1983106055 300 YV 301
Cdd:cd19511   158 YV 159
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 138-301 3.43e-57

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: 185.09  E-value: 3.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKL 217
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 218 VRALFEMARELQPSVVFMDEIDALLSTRsASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRLEK 297
Cdd:cd19523    81 LQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                  ....
gi 1983106055 298 RIYV 301
Cdd:cd19523   160 RLLV 163
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 138-301 5.67e-56

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: 181.72  E-value: 5.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFT--GLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGE 215
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRalGLK-PPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 216 KLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR-- 293
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRRpg 157


                  ....*...
gi 1983106055 294 RLEKRIYV 301
Cdd:cd19503   158 RFDREVEI 165
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 136-301 4.76e-53

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: 174.45  E-value: 4.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 136 WTDIAGLDVAKQILQEAVILPTLRPDLFTGLR-APPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEG 214
Cdd:cd19502     2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 215 EKLVRALFEMARELQPSVVFMDEIDALLSTR----SASENEASRRIKnQFFTELDGAASSqeDRILVMGATNLPQELDEA 290
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsgTGGDREVQRTML-ELLNQLDGFDPR--GNIKVIMATNRPDILDPA 158

                         170
                  ....*....|...
gi 1983106055 291 IIR--RLEKRIYV 301
Cdd:cd19502   159 LLRpgRFDRKIEF 171
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 145-301 1.48e-51

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: 170.37  E-value: 1.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 145 AKQILQEAVILPTLRPDLFTGLRA-PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFE 223
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIrPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 224 MARELQPSVVFMDEIDALLSTR-SASENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQELDEAIIR--RLEKRIY 300
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLIY 158


                  .
gi 1983106055 301 V 301
Cdd:cd19529   159 I 159
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 134-301 6.90e-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: 168.95  E-value: 6.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 134 VHWTDIAGLDVAKQILQEAV-ILptLRPDLFTGLRA-PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWV 211
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVeFL--KNPEKFTKLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 212 GEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASE---NEASRRIKNQFFTELDGAASSqeDRILVMGATNLPQELD 288
Cdd:cd19501    79 GVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLgggHDEREQTLNQLLVEMDGFESN--TGVIVIAATNRPDVLD 156

                         170
                  ....*....|....*
gi 1983106055 289 EAIIR--RLEKRIYV 301
Cdd:cd19501   157 PALLRpgRFDRQVYV 171
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 132-389 2.01e-50

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 180.87  E-value: 2.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 132 PGVHWTDIAGLDVAKQILQEAVILPTLRPDLFTGLR-APPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKW 210
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKY 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 211 VGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEA 290
Cdd:TIGR01243 253 YGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGL--KGRGRVIVIGATNRPDALDPA 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 291 IIR--RLEKRIYVPLPDASSREGLIRhLLSSQKFTLSSREFKHIVKATEGYSGSDLKAVCKDAALGPIREL--GAKVaNV 366
Cdd:TIGR01243 331 LRRpgRFDREIVIRVPDKRARKEILK-VHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFirEGKI-NF 408

                         250       260       270
                  ....*....|....*....|....*....|
gi 1983106055 367 KAEDVRG-------INASDFQVALTRVRPS 389
Cdd:TIGR01243 409 EAEEIPAevlkelkVTMKDFMEALKMVEPS 438
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
136-387 2.77e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 169.68  E-value: 2.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 136 WTDIAGLDVAKQILQEavILPTLR----PDLFtGLrAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWV 211
Cdd:COG1223     1 LDDVVGQEEAKKKLKL--IIKELRrrenLRKF-GL-WPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 212 GEGEKLVRALFEMARELqPSVVFMDEIDALLSTRSASENEA-SRRIKNQFFTELDGAASsqedRILVMGATNLPQELDEA 290
Cdd:COG1223    77 GETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGDQNDVGeVKRVVNALLQELDGLPS----GSVVIAATNHPELLDSA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 291 IIRRLEKRIYVPLPDASSREGLIRHLLssQKFTLS-SREFKHIVKATEGYSGSDLKAVCKDAalgpirelgakVANVKAE 369
Cdd:COG1223   152 LWRRFDEVIEFPLPDKEERKEILELNL--KKFPLPfELDLKKLAKKLEGLSGADIEKVLKTA-----------LKKAILE 218

                         250
                  ....*....|....*...
gi 1983106055 370 DVRGINASDFQVALTRVR 387
Cdd:COG1223   219 DREKVTKEDLEEALKQRK 236
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 128-372 3.06e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 175.34  E-value: 3.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 128 LDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLF--TGLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASS 205
Cdd:PTZ00361  174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYddIGIK-PPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 206 LTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKN---QFFTELDGaASSQEDRILVMgATN 282
Cdd:PTZ00361  253 LIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDG-FDSRGDVKVIM-ATN 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 283 LPQELDEAIIR--RLEKRIYVPLPDASSREGLIRhlLSSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGPIREL 359
Cdd:PTZ00361  331 RIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFE--IHTSKMTLAEDvDLEEFIMAKDELSGADIKAICTEAGLLALRER 408

                         250
                  ....*....|...
gi 1983106055 360 GAKVANvkaEDVR 372
Cdd:PTZ00361  409 RMKVTQ---ADFR 418
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 105-357 1.61e-48

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 169.56  E-value: 1.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 105 RQQQRAGYSKQHAEHAHTILDEV------------LDHSPGVHWTDIAGLDVAKQILQEAVILPTLRPDLFTGLRA-PPR 171
Cdd:PTZ00454  101 RELLKPNASVALHRHSHAVVDILppeadssiqllqMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIdPPR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 172 GVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENE 251
Cdd:PTZ00454  181 GVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 252 ASR---RIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR--RLEKRIYVPLPDASSREgLIRHLLSSqKFTLSS 326
Cdd:PTZ00454  261 ADRevqRILLELLNQMDGF--DQTTNVKVIMATNRADTLDPALLRpgRLDRKIEFPLPDRRQKR-LIFQTITS-KMNLSE 336

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1983106055 327 R-EFKHIVKATEGYSGSDLKAVCKDAALGPIR 357
Cdd:PTZ00454  337 EvDLEDFVSRPEKISAADIAAICQEAGMQAVR 368
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 146-301 2.66e-47

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: 159.21  E-value: 2.66e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 146 KQILQEAVILPTLRPDLFT--GLrAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFE 223
Cdd:cd19528     2 KRELQELVQYPVEHPDKFLkfGM-TPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 224 MARELQPSVVFMDEIDALLSTRSAS---ENEASRRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR--RLEKR 298
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGGNigdAGGAADRVINQILTEMDGM--NTKKNVFIIGATNRPDIIDPAILRpgRLDQL 158


                  ...
gi 1983106055 299 IYV 301
Cdd:cd19528   159 IYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 142-301 1.08e-46

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: 157.65  E-value: 1.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 142 LDVAKQILQEAVILPTLRPDLFTGLR-APPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRA 220
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGiDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 221 LFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQELDEAIIR--RLEKR 298
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSN--VFVIAATNRPDIIDPAMLRpgRLDKT 158


                  ...
gi 1983106055 299 IYV 301
Cdd:cd19530   159 LYV 161
ftsH CHL00176
cell division protein; Validated
 133-403 8.69e-45

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 164.07  E-value: 8.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 133 GVHWTDIAGLDVAKQILQEAVILptLR-PDLFTGLRA-PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKW 210
Cdd:CHL00176  179 GITFRDIAGIEEAKEEFEEVVSF--LKkPERFTAVGAkIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 211 VGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSA---SENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQEL 287
Cdd:CHL00176  257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigGGNDEREQTLNQLLTEMDGFKGNKG--VIVIAATNRVDIL 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 288 DEAIIR--RLEKRIYVPLPDASSREGLIRHLLSSQKFTL-SSREFkhIVKATEGYSGSDLKAVCKDAALgpireLGAKVA 364
Cdd:CHL00176  335 DAALLRpgRFDRQITVSLPDREGRLDILKVHARNKKLSPdVSLEL--IARRTPGFSGADLANLLNEAAI-----LTARRK 407

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1983106055 365 NVKaedvrgINASDFQVALTRVRPSVSSTTIQD-----LVAWNE 403
Cdd:CHL00176  408 KAT------ITMKEIDTAIDRVIAGLEGTPLEDsknkrLIAYHE 445
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
131-386 5.34e-43

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 158.28  E-value: 5.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 131 SPGVHWTDIAGLDVAKQILQEavILPTLR-PDLFTGLRA-PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTS 208
Cdd:COG0465   136 KPKVTFDDVAGVDEAKEELQE--IVDFLKdPEKFTRLGAkIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVE 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 209 KWVGEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSAS------ENEasrRIKNQFFTELDGAASSqeDRILVMGATN 282
Cdd:COG0465   214 MFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggghdERE---QTLNQLLVEMDGFEGN--EGVIVIAATN 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 283 LPQELDEAIIR--RLEKRIYVPLPDASSREGLIR-HllsSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALgpire 358
Cdd:COG0465   289 RPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKvH---ARKKPLAPDvDLEVIARRTPGFSGADLANLVNEAAL----- 360

                         250       260
                  ....*....|....*....|....*...
gi 1983106055 359 LGAKvANVKAedvrgINASDFQVALTRV 386
Cdd:COG0465   361 LAAR-RNKKA-----VTMEDFEEAIDRV 382
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 138-302 2.77e-42

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 146.43  E-value: 2.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFTGLR-APPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEK 216
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 217 LVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR--R 294
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGL--KQRAHVIVMAATNRPNSIDPALRRfgR 158


                  ....*...
gi 1983106055 295 LEKRIYVP 302
Cdd:cd19519   159 FDREIDIG 166
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 138-299 4.68e-42

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: 145.63  E-value: 4.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLF--TGLRaPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGE 215
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFqhLGVE-PPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 216 KLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELD--GAASSQEDRILVMGATNLPQELDEAIIR 293
Cdd:cd19518    80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDelNNEKTAGGPVLVIGATNRPDSLDPALRR 159


                  ....*...
gi 1983106055 294 --RLEKRI 299
Cdd:cd19518   160 agRFDREI 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 138-300 4.87e-39

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: 138.03  E-value: 4.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEAVILPTLRPDLFTGLR-APPRGVLLFGPPGTGKTLLAKAVATEA-----KATFFNISASSLTSKWV 211
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 212 GEGEKLVRALFEMARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQELDEAI 291
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPAL 158

                         170
                  ....*....|.
gi 1983106055 292 IR--RLEKRIY 300
Cdd:cd19517   159 RRpgRFDREFY 169
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 144-301 5.44e-39

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 137.26  E-value: 5.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 144 VAKQILqEAVILPTLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFE 223
Cdd:cd19527     1 VKKEIL-DTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 224 MARELQPSVVFMDEIDALLSTRSASENEAS--RRIKNQFFTELDGAASSQEDrILVMGATNLPQELDEAIIR--RLEKRI 299
Cdd:cd19527    80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSSGQD-VFVIGATNRPDLLDPALLRpgRFDKLL 158


                  ..
gi 1983106055 300 YV 301
Cdd:cd19527   159 YL 160
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
136-357 3.92e-38

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 145.56  E-value: 3.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 136 WTDIAGLDVAKQILQEAVilPTLR-PDLFTGLRAP-PRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGE 213
Cdd:PRK10733  151 FADVAGCDEAKEEVAELV--EYLRePSRFQKLGGKiPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 214 GEKLVRALFEMARELQPSVVFMDEIDALLSTRSA---SENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQELDEA 290
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFEGNEG--IIVIAATNRPDVLDPA 306

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 291 IIR--RLEKRIYVPLPDASSREGLIRhlLSSQKFTLSSR-EFKHIVKATEGYSGSDLKAVCKDAALGPIR 357
Cdd:PRK10733  307 LLRpgRFDRQVVVGLPDVRGREQILK--VHMRRVPLAPDiDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 145-300 3.64e-36

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 129.86  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 145 AKQILQEAVILPTLRPDLFTGLRAP-PRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEGEKLVRALFE 223
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRlRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983106055 224 MARELQPSVVFMDEIDALLSTRSASENEASRRIKNQFFTELDGAASSQEdrILVMGATNLPQELDEAIIR--RLEKRIY 300
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDG--VYVLAATSRPDLIDPALLRpgRLDKLVY 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 140-303 4.50e-27

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: 105.31  E-value: 4.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 140 AGLDVAKQILQEAVILPtlrpdlftglraPPRGVLLFGPPGTGKTLLAKAVATEA---KATFFNISASSLTSKWVGEGEK 216
Cdd:cd00009     1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 217 ---LVRALFEMARELQPSVVFMDEIDALlstrSASENEASRRIKNQFFTELDgaassQEDRILVMGATN--LPQELDEAI 291
Cdd:cd00009    69 ghfLVRLLFELAEKAKPGVLFIDEIDSL----SRGAQNALLRVLETLNDLRI-----DRENVRVIGATNrpLLGDLDRAL 139

                         170
                  ....*....|..
gi 1983106055 292 IRRLEKRIYVPL 303
Cdd:cd00009   140 YDRLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 171-301 1.53e-20

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: 88.32  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATEAKATFFNI-SASSLTSKWVGEGEKLVRALFEMARELQPS--------VVFMDEIDAL 241
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983106055 242 LSTRSASENEAS--RRIKNQFFTELDGAasSQEDRILVMGATNLPQELDEAIIR--RLEKRIYV 301
Cdd:cd19504   116 CKQRGSMAGSTGvhDTVVNQLLSKIDGV--EQLNNILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 169-305 6.91e-20

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 85.50  E-value: 6.91e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055  169 PPRGVLLFGPPGTGKTLLAKAVATEAKAT---FFNISASSLTS--------------KWVGEGEKLVRALFEMARELQPS 231
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983106055  232 VVFMDEIDALLSTRSASENEASRRIKNQFFTEldgaassQEDRILVMGATNLPQELDEAIIR-RLEKRIYVPLPD 305
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLK-------SEKNLTVILTTNDEKDLGPALLRrRFDRRIVLLLIL 148
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 138-294 1.93e-17

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 78.95  E-value: 1.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 138 DIAGLDVAKQILQEavilptlRPDLFT------GLrAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWV 211
Cdd:cd19507     1 DVGGLDNLKDWLKK-------RKAAFSkqasayGL-PTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 212 GEGEKLVRALFEMARELQPSVVFMDEID-ALLSTRSASENEASRRIKNQFFTELdgaaSSQEDRILVMGATNLPQELDEA 290
Cdd:cd19507    73 GESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWL----QEKKKPVFVVATANNVQSLPPE 148


                  ....
gi 1983106055 291 IIRR 294
Cdd:cd19507   149 LLRK 152
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 171-301 3.59e-17

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 79.41  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVA---------TEAKATFFNISASSLTSKWVGEGEKLVRALFEMAREL---QPSVVF--MD 236
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAqklsirlssRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlID 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983106055 237 EIDALLSTRSA--SENEASR--RIKNQFFTELDGAASSqeDRILVMGATNLPQELDEAIIRRLEKRIYV 301
Cdd:cd19508   133 EVESLAAARSAssSGTEPSDaiRVVNAVLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 146-299 6.61e-16

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: 74.87  E-value: 6.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 146 KQILQEAVILPtLRPDLFTGLRAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKWVGEG--EKLVRALFE 223
Cdd:cd19506     3 RQLLTLYGILP-LGSQAVHEKAPLVKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLK 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055 224 MARELQPSVVFMDEIDALLSTRSASENEAS--RRIKNQFFTELDGAASsqEDRILVMGATNLPQELDEAIIRRLEKRI 299
Cdd:cd19506    82 VARQLQPSVIWIGDAEKTFYKKVPKTEKQLdpKRLKKDLPKILKSLKP--EDRVLIVGTTSRPFEADLKSFCKVYNKI 157
ycf46 CHL00195
Ycf46; Provisional
 137-345 1.76e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 78.14  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 137 TDIAGLDVAKQILQeavilptLRPDLFT------GLRAPpRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKW 210
Cdd:CHL00195  228 SDIGGLDNLKDWLK-------KRSTSFSkqasnyGLPTP-RGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 211 VGEGEKLVRALFEMARELQPSVVFMDEID-ALLSTRSASENEASRRIKNQFFTELdgaaSSQEDRILVMGATNLPQELDE 289
Cdd:CHL00195  300 VGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWL----SEKKSPVFVVATANNIDLLPL 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1983106055 290 AIIR--RLEKRIYVPLPDASSREGLIR-HLLSSQKFTLSSREFKHIVKATEGYSGSDLK 345
Cdd:CHL00195  376 EILRkgRFDEIFFLDLPSLEEREKIFKiHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIE 434
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 171-301 7.98e-15

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: 71.23  E-value: 7.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATEAKATF--FNISASSLTSkwvgegeKLVRALfeMARELQPSVVFMDEIDALLSTRSA- 247
Cdd:cd19510    24 RGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSEVVLTD-------DRLNHL--LNTAPKQSIILLEDIDAAFESREHn 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1983106055 248 -----SENEASRRIKNQFFTELDGAASSQEdRILVMgATNLPQELDEAIIR--RLEKRIYV 301
Cdd:cd19510    95 kknpsAYGGLSRVTFSGLLNALDGVASSEE-RIVFM-TTNHIERLDPALIRpgRVDMKIYM 153
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 167-299 3.25e-12

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: 64.08  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 167 RAPPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSkwVG-EGEKLVRALFEMARELQPS-VVFMDEIDALLST 244
Cdd:cd19512    19 KGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAIHKVFDWANTSRRGlLLFVDEADAFLRK 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983106055 245 RSASE-NEASRRIKNQFFTEldgaASSQEDRILVMGATNLPQELDEAIIRRLEKRI 299
Cdd:cd19512    97 RSTEKiSEDLRAALNAFLYR----TGEQSNKFMLVLASNQPEQFDWAINDRIDEMV 148
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 173-242 2.54e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 65.08  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISAssltskwVGEGEKLVRALFEMAREL----QPSVVFMDEI--------DA 240
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERraygRRTILFVDEIhrfnkaqqDA 124


                  ..
gi 1983106055 241 LL 242
Cdd:COG2256   125 LL 126
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 10-75 2.95e-11

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: 58.71  E-value: 2.95e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983106055  10 EDAIQKtIEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKD 75
Cdd:pfam04212   2 SKALEL-VKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 169-301 1.89e-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: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 169 PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTSKW--------------VGEGEKLVRALFEMARELQPSVVF 234
Cdd:cd19505    11 PSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKpdfgnddwidgmliLKESLHRLNLQFELAKAMSPCIIW 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983106055 235 MDEIDALLSTRSASENEASRR----IKNQFFTELDGAASSQEdrILVMGATNLPQELDEAII--RRLEKRIYV 301
Cdd:cd19505    91 IPNIHELNVNRSTQNLEEDPKlllgLLLNYLSRDFEKSSTRN--ILVIASTHIPQKVDPALIapNRLDTCINI 161
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 173-242 1.93e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 62.02  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSltskwvgEGEKLVRALFEMAREL----QPSVVFMDEI--------DA 240
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEIhrfnkaqqDA 111


                  ..
gi 1983106055 241 LL 242
Cdd:PRK13342  112 LL 113
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 11-82 2.96e-10

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: 56.12  E-value: 2.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983106055  11 DAIQKTIEE---AVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKDWMAEQAR 82
Cdd:cd02678     1 DFLQKAIELvkkAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 17-75 1.69e-09

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: 53.85  E-value: 1.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1983106055  17 IEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKD 75
Cdd:cd02656    10 IKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKE 68
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 20-74 3.09e-09

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: 53.20  E-value: 3.09e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1983106055  20 AVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLK 74
Cdd:cd02683    13 AVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKNLRQKISEYMDRAEAIK 67
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 170-254 1.26e-08

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: 54.31  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 170 PRGVLLFGPPGTGKTLLAKAVATEAKATFFNISASSLTS-KWVGegeklvRALFEMARELQPSVVFMDEIDALLSTRSAS 248
Cdd:cd19498    46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVG------RDVESIIRDLVEGIVFIDEIDKIAKRGGSS 119


                  ....*.
gi 1983106055 249 ENEASR 254
Cdd:cd19498   120 GPDVSR 125
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 328-363 2.74e-07

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: 46.76  E-value: 2.74e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1983106055 328 EFKHIVKATEGYSGSDLKAVCKDAALGPIRELGAKV 363
Cdd:pfam17862   3 DLEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
17-74 2.45e-06

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 44.99  E-value: 2.45e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055   17 IEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLK 74
Cdd:smart00745  12 ISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIK 69
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
171-221 4.77e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.43  E-value: 4.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATE--AKATFFNISASSLTSKWVGEGEKLVRAL 221
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEFLMQAL 117
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 171-280 8.29e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 47.92  E-value: 8.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATE-------AKATFFNISASSLTSKWVGEGEKLVRALFEMARElqpSVVFMDEIDALLS 243
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVE 389

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1983106055 244 TRSASENEASRRIKNQFFTELDgaasSQEDRILVMGA 280
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARME----NDRDRLVVIGA 422
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 170-239 1.61e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.88  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 170 PRGVLLF-GPPGTGKTLLAKAVATE---AKATFFNISASSLT-----SKWVGEGEKLVRA-----LFEMARELQPSVVFM 235
Cdd:pfam07724   2 PIGSFLFlGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggqLTEAVRRKPYSIVLI 81


                  ....
gi 1983106055 236 DEID 239
Cdd:pfam07724  82 DEIE 85
MIT_AAA_Arch cd02682
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 10-74 3.21e-05

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


Pssm-ID: 239145  Cd Length: 75  Bit Score: 41.75  E-value: 3.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983106055  10 EDAIQKTIEEAVAVDKAGKYAEAVELYASGIEkMMTQMAQL-PNEEAKTHMRHKINEYMLRAEYLK 74
Cdd:cd02682     3 EEMARKYAINAVKAEKEGNAEDAITNYKKAIE-VLSQIVKNyPDSPTRLIYEQMINEYKRRIEVLE 67
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 171-221 3.21e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.76  E-value: 3.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATE--AKATFFNISASSLTSKWVGEGEKLVRAL 221
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEALTQAF 103
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 173-239 3.57e-05

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.90  E-value: 3.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSLT-SKWVGEG-----EKLVR-ALFEMARElQPSVVFMDEID 239
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvenilLKLLQaADYDVERA-QRGIVYIDEID 125
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 172-295 3.94e-05

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: 43.05  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 172 GVLLFGPPGTGKTLLAKAVA----------------TEAKATFFNISASSLTSKWVgEGEkLVRAlfemARElqPSVVFM 235
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqltrdTTEEDLFGRRNIDPGGASWV-DGP-LVRA----ARE--GEIAVL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983106055 236 DEIdallstrsaseNEASRRIKNQFFT----------ELDGAASSQEDRILVMGATNLP----QELDEAIIRRL 295
Cdd:pfam07728  73 DEI-----------NRANPDVLNSLLSllderrlllpDGGELVKAAPDGFRLIATMNPLdrglNELSPALRSRF 135
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
173-241 6.49e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 44.74  E-value: 6.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSLtskwvgegEK---LVRALfemaRELQP-SVVFMDEIDAL 241
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL--------EKpgdLAAIL----TNLEEgDVLFIDEIHRL 114
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 144-315 7.38e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.39  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 144 VAKQIL-QEAVILptlrpDLFTGLRAppRG-VLLFGPPGTGKTLLAKAVATEAKATFF--NISASSLTSKWVGEgEKLVR 219
Cdd:COG0714    10 IGKVYVgQEELIE-----LVLIALLA--GGhLLLEGVPGVGKTTLAKALARALGLPFIriQFTPDLLPSDILGT-YIYDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 220 AlfEMARELQP-----SVVFMDEID--------ALLstrsasenEA-SRRiknQFftELDGAASSQEDRILVMGATNlPQ 285
Cdd:COG0714    82 Q--TGEFEFRPgplfaNVLLADEINrappktqsALL--------EAmEER---QV--TIPGGTYKLPEPFLVIATQN-PI 145

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1983106055 286 E------LDEAIIRRLEKRIYVPLPDASS-REGLIRH 315
Cdd:COG0714   146 EqegtypLPEAQLDRFLLKLYIGYPDAEEeREILRRH 182
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
 119-241 1.72e-04

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: 42.16  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 119 HAHTILDEvlDHspgvhwtdiAGLDVAKQILQEAVILPTLRPDLftglRAPprgVLLF-GPPGTGKTLLAKAVATEAKAT 197
Cdd:cd19500     3 KARKVLDA--DH---------YGLEDVKERILEYLAVRKLKGSM----KGP---ILCLvGPPGVGKTSLGKSIARALGRK 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055 198 FFNISASSLTSkwvgEGE--------------KLVRALFEmARELQPsVVFMDEIDAL 241
Cdd:cd19500    65 FVRISLGGVRD----EAEirghrrtyvgampgRIIQALKK-AGTNNP-VFLLDEIDKI 116
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 173-238 1.76e-04

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: 41.72  E-value: 1.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKAtffNISASSltskwvgeGEKLVRA--LFEMARELQP-SVVFMDEI 238
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGV---NIRITS--------GPAIERPgdLAAILTNLEPgDVLFIDEI 93
PRK13341 PRK13341
AAA family ATPase;
174-243 2.20e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 43.50  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 174 LLFGPPGTGKTLLAKAVATEAKATFFNISAssltskwVGEGEKLVRALFEMAREL-----QPSVVFMDEI--------DA 240
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKERlerhgKRTILFIDEVhrfnkaqqDA 128


                  ...
gi 1983106055 241 LLS 243
Cdd:PRK13341  129 LLP 131
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 173-249 2.20e-04

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.46  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVA-----TEAKATFFNISASSLTSKWVGE----------GEK----LVRALFemareLQPSVV 233
Cdd:cd00267    28 VALVGPNGSGKSTLLRAIAgllkpTSGEILIDGKDIAKLPLEELRRrigyvpqlsgGQRqrvaLARALL-----LNPDLL 102

                          90
                  ....*....|....*.
gi 1983106055 234 FMDEIDALLSTRSASE 249
Cdd:cd00267   103 LLDEPTSGLDPASRER 118
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
158-302 2.65e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 158 LRPdLFTGlrAPPRGVLLFGPPGTGKTLLAKAVATEAKA--------------------TFFNIsASSLTSKwVGEGE-- 215
Cdd:COG1474    42 LRP-ALRG--ERPSNVLIYGPTGTGKTAVAKYVLEELEEeaeergvdvrvvyvncrqasTRYRV-LSRILEE-LGSGEdi 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 216 --------KLVRALFEMARELQPSVVF-MDEIDALLStRSASE--NEASRriknqFFTELDGAassqedRILVMGATN-- 282
Cdd:COG1474   117 pstglstdELFDRLYEALDERDGVLVVvLDEIDYLVD-DEGDDllYQLLR-----ANEELEGA------RVGVIGISNdl 184

                         170       180
                  ....*....|....*....|..
gi 1983106055 283 -LPQELDEAIIRRL-EKRIYVP 302
Cdd:COG1474   185 eFLENLDPRVKSSLgEEEIVFP 206
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
 118-202 4.11e-04

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 42.70  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 118 EHAHTILDEvlDHspgvhwtdiAGLDVAKQ-ILqE--AVIlpTLRPDLftglRAPprgVLLF-GPPGTGKTLLAKAVate 193
Cdd:COG0466   317 KKAEKILDE--DH---------YGLEKVKErIL-EylAVR--KLKKKL----KGP---ILCLvGPPGVGKTSLGKSI--- 372

                          90
                  ....*....|..
gi 1983106055 194 AKAT---FFNIS 202
Cdd:COG0466   373 ARALgrkFVRIS 384
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 165-239 4.11e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 41.01  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 165 GLRAP--PRGVLLF-GPPGTGKTLLAKAVA-----TEAKATFFNISA-------SSLTS---KWVGEGEKLVraLFEMAR 226
Cdd:cd19499    33 GLSDPnrPIGSFLFlGPTGVGKTELAKALAellfgDEDNLIRIDMSEymekhsvSRLIGappGYVGYTEGGQ--LTEAVR 110

                          90
                  ....*....|...
gi 1983106055 227 ELQPSVVFMDEID 239
Cdd:cd19499   111 RKPYSVVLLDEIE 123
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 173-267 7.00e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 39.02  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFN-ISASSLtskwvgegEKLVRALFEMARELQPSVVFMDEIDALLstrSASENE 251
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQALLSDEPvIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLA---RASQGD 69

                          90
                  ....*....|....*.
gi 1983106055 252 ASRRIKNQFFTELDGA 267
Cdd:cd01120    70 RSSELLEDLAKLLRAA 85
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 170-295 1.01e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.79  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 170 PRGVLLFGPPGTGKTLLAKAV---ATEAKATFFNISASSLTSKWVG----EGEKLVRALFEMARELQPSvVFMDEIDALL 242
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGLLRQLLDELESSLLE-AWRAALLEAL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1983106055 243 STRSASENEASRRIKNQFFTELDGAASSQEDRILVMGATNLPQELDEAIIRRL 295
Cdd:pfam13191 103 APVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDLQWADEASLQLLAAL 155
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
171-194 1.60e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 1.60e-03
                          10        20
                  ....*....|....*....|....
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATEA 194
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEA 123
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 17-79 1.65e-03

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: 37.10  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983106055  17 IEEAVAVDKAGKYAEAVELYASGIEKMMTQMAQLPNEEAKTHMRHKINEYMLRAEYLKDWMAE 79
Cdd:cd02684    10 VVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEELKALIAS 72
PRK04195 PRK04195
replication factor C large subunit; Provisional
 169-241 1.74e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 40.29  E-value: 1.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983106055 169 PPRGVLLFGPPGTGKTLLAKAVATEAKATFFNISAS-----SLTSKWVGEGEKlVRALFEMARELqpsvVFMDEIDAL 241
Cdd:PRK04195   38 PKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIERVAGEAAT-SGSLFGARRKL----ILLDEVDGI 110
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 161-191 1.79e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.52  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1983106055 161 DLFTGLRAPPrGVLLFGPPGTGKTLLAKAVA 191
Cdd:COG1401   213 AFLAALKTKK-NVILAGPPGTGKTYLARRLA 242
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 173-241 1.99e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 39.98  E-value: 1.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKATFFNISASSLtskwvgegEKlVRALFEMARELQP-SVVFMDEIDAL 241
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL--------EK-PGDLAAILTNLEEgDVLFIDEIHRL 93
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 173-194 2.30e-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: 39.38  E-value: 2.30e-03
                          10        20
                  ....*....|....*....|..
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEA 194
Cdd:NF038214   93 VLLLGPPGTGKTHLAIALGYAA 114
PRK08116 PRK08116
hypothetical protein; Validated
 171-193 3.27e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.85  E-value: 3.27e-03
                          10        20
                  ....*....|....*....|...
gi 1983106055 171 RGVLLFGPPGTGKTLLAKAVATE 193
Cdd:PRK08116  115 VGLLLWGSVGTGKTYLAACIANE 137
PRK12422 PRK12422
chromosomal replication initiator protein DnaA;
143-327 3.86e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 183521 [Multi-domain]  Cd Length: 445  Bit Score: 39.43  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 143 DVAKQILQEAvilpTLRPDLFTGLRAPPrgVLLFGPPGTGKTLLAKAVAT---EAKATFFNISASSLTskwvgegEKLVR 219
Cdd:PRK12422  120 DLPHRILQEF----TKVSEQGKGFPFNP--IYLFGPEGSGKTHLMQAAVHalrESGGKILYVRSELFT-------EHLVS 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 220 ALF--EMARELQP----SVVFMDEIDaLLSTRSASENEasrriknqFFTELDGAASsqEDRILVMGATNLPQEL---DEA 290
Cdd:PRK12422  187 AIRsgEMQRFRQFyrnvDALFIEDIE-VFSGKGATQEE--------FFHTFNSLHT--EGKLIVISSTCAPQDLkamEER 255

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1983106055 291 IIRRLEKRIYVPLpDASSREGLiRHLLSSQKFTLSSR 327
Cdd:PRK12422  256 LISRFEWGIAIPL-HPLTKEGL-RSFLERKAEALSIR 290
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
173-239 4.15e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 38.99  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVA-------TEAKATffnisasSLT-SKWVGEG-E----KLV-RALFEMARElQPSVVFMDEI 238
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLArildvpfAIADAT-------TLTeAGYVGEDvEnillKLLqAADYDVEKA-QRGIVYIDEI 182


                  .
gi 1983106055 239 D 239
Cdd:PRK05342  183 D 183
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 169-189 7.56e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 38.55  E-value: 7.56e-03
                          10        20
                  ....*....|....*....|...
gi 1983106055 169 PPRG--VLLFGPPGTGKTLLAKA 189
Cdd:COG1221   127 PPKGlhTLILGPTGVGKSFFAEL 149
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 173-192 7.64e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.51  E-value: 7.64e-03
                          10        20
                  ....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVAT 192
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRLPG 44
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 173-238 7.97e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.14  E-value: 7.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVATEAKAtffNISASS-------------LTSkwvgegeklvralfemareLQP-SVVFMDEI 238
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGV---NIRITSgpaiekpgdlaaiLTN-------------------LEEgDVLFIDEI 114
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 173-192 9.44e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 38.10  E-value: 9.44e-03
                          10        20
                  ....*....|....*....|
gi 1983106055 173 VLLFGPPGTGKTLLAKAVAT 192
Cdd:COG0606   214 LLMIGPPGSGKTMLARRLPG 233
 
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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