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Conserved domains on  [gi|568911103|ref|XP_006497027|]
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nuclear valosin-containing protein-like isoform X2 [Mus musculus]

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 1001098)

CDC48 family AAA ATPase is involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus; similar to yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
137-750 0e+00

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.


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  137 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 215
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  216 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 295
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  296 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 375
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  376 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 455
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  456 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 535
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  536 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 614
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  615 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 694
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103  695 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 750
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
137-750 0e+00

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: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  137 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 215
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  216 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 295
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  296 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 375
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  376 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 455
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  456 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 535
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  536 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 614
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  615 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 694
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103  695 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 750
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
160-326 3.05e-108

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: 326.67  E-value: 3.05e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 238
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 239 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 317
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 568911103 318 GRFDREVCL 326
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
401-734 4.36e-107

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 329.66  E-value: 4.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 401 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 480
Cdd:COG1222    8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 481 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 560
Cdd:COG1222   84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 561 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:COG1222  164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 640 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 719
Cdd:COG1222  244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                        330
                 ....*....|....*
gi 568911103 720 KHFEDAFKKVKPSIS 734
Cdd:COG1222  308 EDLEKAIEKVKKKTE 322
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
447-741 2.46e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 2.46e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 447 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 520
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 521 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 597
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 598 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 676
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 677 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 741
Cdd:PRK03992 333 T--EGASGADLKAICTEAGMFAIRDDRTE-----------VTMEDFLKAIEKVmgkeEKDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
512-642 2.40e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 188.57  E-value: 2.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 591
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568911103  592 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 642
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
470-743 9.03e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 181.86  E-value: 9.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 621
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 622 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 701
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568911103 702 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 743
Cdd:NF041006 327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
cell_div_CdvC NF041006
cell division protein CdvC;
155-380 4.38e-37

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.95  E-value: 4.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 155 NVKFEDVGG-NDAtlKEVCKMLI--HMRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSG 231
Cdd:NF041006  99 KVTFSDIVGlEDV--KEALKEAIvyPSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 232 VSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGAT 304
Cdd:NF041006 174 WLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGAT 250
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103 305 NRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 380
Cdd:NF041006 251 NKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
508-643 1.09e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.19  E-value: 1.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103   508 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 570
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103   571 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 643
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
137-750 0e+00

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: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  137 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 215
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  216 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 295
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  296 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 375
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  376 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 455
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  456 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 535
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  536 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 614
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  615 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 694
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103  695 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 750
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
160-326 3.05e-108

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: 326.67  E-value: 3.05e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 238
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 239 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 317
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 568911103 318 GRFDREVCL 326
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
401-734 4.36e-107

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 329.66  E-value: 4.36e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 401 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 480
Cdd:COG1222    8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 481 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 560
Cdd:COG1222   84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 561 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:COG1222  164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 640 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 719
Cdd:COG1222  244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                        330
                 ....*....|....*
gi 568911103 720 KHFEDAFKKVKPSIS 734
Cdd:COG1222  308 EDLEKAIEKVKKKTE 322
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
480-640 1.26e-101

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: 309.42  E-value: 1.26e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 480 LEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 559
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 560 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 568911103 640 V 640
Cdd:cd19530  161 V 161
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
483-640 8.34e-92

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: 283.41  E-value: 8.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 483 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 562
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 563 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 640
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
148-380 1.27e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 281.51  E-value: 1.27e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 148 STELQISNVKFEDVGGNDATLKEVCKMLI-HMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP 226
Cdd:COG1222   67 AVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 227 EIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATN 305
Cdd:COG1222  147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATN 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911103 306 RPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 380
Cdd:COG1222  224 RPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
382-730 4.54e-83

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: 269.47  E-value: 4.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 382 RVLMKQQAQQKKKPEIEGLPSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSA 461
Cdd:COG0464   64 ALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 462 KREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVK 541
Cdd:COG0464  144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 542 GPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLetRQQVFILAATNRP 621
Cdd:COG0464  224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRP 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 622 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 701
Cdd:COG0464  302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL 374
                        330       340
                 ....*....|....*....|....*....
gi 568911103 702 eitaqkngvgaGELKVSHKHFEDAFKKVK 730
Cdd:COG0464  375 -----------GREPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
447-741 2.46e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 2.46e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 447 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 520
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 521 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 597
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 598 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 676
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 677 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 741
Cdd:PRK03992 333 T--EGASGADLKAICTEAGMFAIRDDRTE-----------VTMEDFLKAIEKVmgkeEKDSMEEPGVMF 388
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
160-326 3.76e-76

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: 242.58  E-value: 3.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 237
Cdd:cd19503    1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 238 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRA 317
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS---RGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 568911103 318 GRFDREVCL 326
Cdd:cd19503  157 GRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
158-380 3.59e-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: 240.58  E-value: 3.59e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 158 FEDVGGNDATLKEVCKMLIHMRH-PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 236
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 237 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRR 316
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRS-----DVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911103 317 agRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 380
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
483-640 5.26e-70

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: 226.22  E-value: 5.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 483 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 562
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 563 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 640
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
483-640 1.95e-69

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: 224.70  E-value: 1.95e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 483 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 562
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 563 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 568911103 640 V 640
Cdd:cd19528  161 I 161
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
476-636 5.94e-68

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: 221.01  E-value: 5.94e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 555
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 556 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 635
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 .
gi 568911103 636 K 636
Cdd:cd19503  161 R 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
470-729 3.01e-67

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 230.25  E-value: 3.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  470 PNVTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  550 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRP 621
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  622 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 701
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVAR--RTPGFSGADLANLLNEAALLAARK 278
                         250       260
                  ....*....|....*....|....*...
gi 568911103  702 EITAqkngvgagelkVSHKHFEDAFKKV 729
Cdd:TIGR01241 279 NKTE-----------ITMNDIEEAIDRV 295
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
160-327 1.24e-66

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: 217.69  E-value: 1.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 238
Cdd:cd19519    1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 239 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAG 318
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK---QRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 568911103 319 RFDREVCLG 327
Cdd:cd19519  158 RFDREIDIG 166
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
483-639 1.63e-66

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: 216.91  E-value: 1.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 483 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 562
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103 563 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
142-380 8.84e-65

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 220.47  E-value: 8.84e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 142 KKAKARSTELQIS-NVKFEDVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDL 218
Cdd:PRK03992 113 KDPRVQAMEVIESpNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNA 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 219 PILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaT 295
Cdd:PRK03992 192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---R 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 296 ARVLVIGATNRPDSLDPALRRAGRFDR--EVCLgiPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCR 373
Cdd:PRK03992 269 GNVKIIAATNRIDILDPAILRPGRFDRiiEVPL--PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICT 346

                 ....*..
gi 568911103 374 EAAMCAV 380
Cdd:PRK03992 347 EAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
143-382 4.57e-64

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 221.78  E-value: 4.57e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  143 KAKARSTELQISNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 222
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  223 VAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKRE---VASKDMERRIVAQLLTCMDDLNNvaaTARVL 299
Cdd:TIGR01241 119 ISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT---NTGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  300 VIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCA 379
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275

                  ...
gi 568911103  380 VNR 382
Cdd:TIGR01241 276 ARK 278
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
479-640 2.76e-62

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: 205.59  E-value: 2.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 479 ALEDIRDelimaILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 558
Cdd:cd19481    1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 559 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKT 637
Cdd:cd19481   76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                 ...
gi 568911103 638 LFV 640
Cdd:cd19481  156 IEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
470-729 5.60e-62

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 218.37  E-value: 5.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADI-GA------LEDIRDELimailapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKG 542
Cdd:COG0465  137 PKVTFDDVaGVdeakeeLQEIVDFL--------KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 543 PELLNMYVG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLETRQQV 612
Cdd:COG0465  209 SDFVEMFVGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGV 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 613 FILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtKpPLDEDVNLETIANdlRCNCYTGADLTALVR 692
Cdd:COG0465  282 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIAR--RTPGFSGADLANLVN 356
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568911103 693 EASLCALRqeitaqkngvgAGELKVSHKHFEDAFKKV 729
Cdd:COG0465  357 EAALLAAR-----------RNKKAVTMEDFEEAIDRV 382
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
143-382 3.31e-60

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 213.36  E-value: 3.31e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 143 KAKARSTELQISNVKFEDVGGND---ATLKEVCKMLihmRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLP 219
Cdd:COG0465  126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 220 ILKVAAPEIVS---GVsGESeqKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDmER-RIVAQLLTCMD--Dln 290
Cdd:COG0465  203 FFSISGSDFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGHD-EReQTLNQLLVEMDgfE-- 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 291 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 370
Cdd:COG0465  277 ---GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353
                        250
                 ....*....|..
gi 568911103 371 LCREAAMCAVNR 382
Cdd:COG0465  354 LVNEAALLAARR 365
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
473-636 7.23e-60

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: 199.49  E-value: 7.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 473 TWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 552
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 553 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAIL 629
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*..
gi 568911103 630 RPGRLDK 636
Cdd:cd19502  161 RPGRFDR 167
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
483-640 8.30e-60

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: 198.89  E-value: 8.30e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 483 IRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 562
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 563 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-TRQQVFILAATNRPDIIDPAILRPGRLDKTLF 639
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                 .
gi 568911103 640 V 640
Cdd:cd19527  160 L 160
ftsH CHL00176
cell division protein; Validated
472-729 1.27e-59

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 212.99  E-value: 1.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 472 VTWADIGALEDIRDEL--IMAILapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFeeVVSFL---KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLETRQQVFILAATNRP 621
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRV 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 622 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 701
Cdd:CHL00176 332 DILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARR 406
                        250       260
                 ....*....|....*....|....*...
gi 568911103 702 EITaqkngvgagelKVSHKHFEDAFKKV 729
Cdd:CHL00176 407 KKA-----------TITMKEIDTAIDRV 423
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
472-640 1.05e-58

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: 196.30  E-value: 1.05e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 472 VTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 551
Cdd:cd19501    1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 552 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAI 628
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 568911103 629 LRPGRLDKTLFV 640
Cdd:cd19501  160 LRPGRFDRQVYV 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
158-375 5.57e-58

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 197.41  E-value: 5.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 158 FEDVGGNDATlKEVCKMLIH-MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 236
Cdd:COG1223    1 LDDVVGQEEA-KKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 237 EQKLRELFDQAvSNAPCIVFIDEIDAITPKREVASKDME-RRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALR 315
Cdd:COG1223   80 ARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDGLPS-----GSVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 316 RagRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 375
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
427-667 1.95e-57

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 204.17  E-value: 1.95e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  427 GLLRDQDPLSEEQMQGLCIELndfiVALAEVQPSAKREgfvtVPNVTWADIGAL----EDIRDelimAILAPVRNPDQFR 502
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEA----IPRTEVEDLVLEE----VPDVTYADIGGLgsqiEQIRD----AVELPFLHPELYR 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  503 TLGLGTPAGILLAGPPGCGKTLLAKAVAN-------ESGLN---FISVKGPELLNMYVGESERAVRQVFQRAKNSA---- 568
Cdd:TIGR03689 210 EYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegr 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  569 PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLP 643
Cdd:TIGR03689 290 PVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERP 365
                         250       260
                  ....*....|....*....|....*
gi 568911103  644 PPADRVAIL-KTITKNgtkPPLDED 667
Cdd:TIGR03689 366 DAEAAADIFaKYLTDD---LPLPED 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
512-642 2.40e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 188.57  E-value: 2.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 591
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568911103  592 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 642
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
470-729 2.55e-56

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 197.68  E-value: 2.55e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 626
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 627 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRqeitaq 706
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAICQEAGMQAVR------ 368
                        250       260
                 ....*....|....*....|...
gi 568911103 707 KNgvgagELKVSHKHFEDAFKKV 729
Cdd:PTZ00454 369 KN-----RYVILPKDFEKGYKTV 386
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
476-641 4.83e-56

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: 189.18  E-value: 4.83e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 555
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 556 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 635
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 568911103 636 KTLFVG 641
Cdd:cd19519  161 REIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
177-324 5.65e-55

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: 185.95  E-value: 5.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 177 HMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVF 256
Cdd:cd19481   12 PRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILF 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 257 IDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREV 324
Cdd:cd19481   91 IDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
473-747 3.02e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 197.95  E-value: 3.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 473 TWADIGALEDIRDElIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 552
Cdd:PRK10733 150 TFADVAGCDEAKEE-VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 553 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLETRQQVFILAATNRPDII 624
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 625 DPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDlrCNCYTGADLTALVREASLCALRqeit 704
Cdd:PRK10733 304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 568911103 705 aqkngvgAGELKVSHKHFEDAFKKVKPSISIKDQVMYEALQRS 747
Cdd:PRK10733 375 -------GNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
168-322 5.11e-54

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 183.25  E-value: 5.11e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 168 LKEVCKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFD 245
Cdd:cd19511    1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911103 246 QAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
143-379 1.92e-53

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 196.02  E-value: 1.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 143 KAKARS-TELQISNVkFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPIL 221
Cdd:PRK10733 136 KSKARMlTEDQIKTT-FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 222 KVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREV---ASKDMERRIVAQLLTCMDDLNnvaATARV 298
Cdd:PRK10733 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE---GNEGI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 299 LVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMC 378
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371

                 .
gi 568911103 379 A 379
Cdd:PRK10733 372 A 372
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
195-327 2.49e-52

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: 177.40  E-value: 2.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDM 274
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568911103  275 ERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREVCLG 327
Cdd:pfam00004  81 SRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
ftsH CHL00176
cell division protein; Validated
134-382 3.09e-52

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.19  E-value: 3.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 134 GEIEALLQKKAKarstelqiSNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIA 213
Cdd:CHL00176 166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 214 GELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDMER-RIVAQLLTCMDDLN 290
Cdd:CHL00176 238 GEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEReQTLNQLLTEMDGFK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 291 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 370
Cdd:CHL00176 318 ---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLAN 394
                        250
                 ....*....|..
gi 568911103 371 LCREAAMCAVNR 382
Cdd:CHL00176 395 LLNEAAILTARR 406
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
156-324 5.68e-52

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: 178.19  E-value: 5.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 156 VKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 235
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 236 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDMERRIVAQLLTCMDDLnnvAATARVLVIGATNRPDSLDP 312
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGF---ESNTGVIVIAATNRPDVLDP 157
                        170
                 ....*....|..
gi 568911103 313 ALRRAGRFDREV 324
Cdd:cd19501  158 ALLRPGRFDRQV 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
491-730 4.76e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 178.15  E-value: 4.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 491 ILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNsAPC 570
Cdd:COG1223   17 IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFARR-APC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 571 VIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLetRQQVFILAATNRPDIIDPAILRpgRLDKTLFVGLPPPADRV 649
Cdd:COG1223   96 VIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 650 AILKtitKNGTKPPLDEDVNLETIANdlRCNCYTGADLTALVREaslcALRQEITAQKNgvgagelKVSHKHFEDAFKKV 729
Cdd:COG1223  172 EILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----ALKKAILEDRE-------KVTKEDLEEALKQR 235

                 .
gi 568911103 730 K 730
Cdd:COG1223  236 K 236
cell_div_CdvC NF041006
cell division protein CdvC;
470-743 9.03e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 181.86  E-value: 9.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 621
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 622 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 701
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 568911103 702 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 743
Cdd:NF041006 327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
476-636 2.39e-50

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: 173.74  E-value: 2.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 555
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 556 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----ETRQQVFILAATNRPDIIDPAILRP 631
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*
gi 568911103 632 GRLDK 636
Cdd:cd19518  161 GRFDR 165
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
477-640 4.60e-50

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: 172.54  E-value: 4.60e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 477 IGALEDIRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 556
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 557 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpgRL 634
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 568911103 635 DKTLFV 640
Cdd:cd19509  158 EKRIYI 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
155-382 1.54e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 179.19  E-value: 1.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 155 NVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVS 233
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 234 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMER---RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSL 310
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQ---TTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911103 311 DPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAVNR 382
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
158-324 2.15e-49

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: 170.98  E-value: 2.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 158 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 236
Cdd:cd19502    2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 237 EQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPA 313
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFD---PRGNIKVIMATNRPDILDPA 158
                        170
                 ....*....|.
gi 568911103 314 LRRAGRFDREV 324
Cdd:cd19502  159 LLRPGRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
178-324 6.88e-48

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 166.52  E-value: 6.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 178 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 257
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911103 258 DEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREV 324
Cdd:cd19529   93 DEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDIIDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
158-380 5.84e-47

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 173.03  E-value: 5.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 158 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 236
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 237 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 316
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911103 317 AGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 380
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
470-729 2.09e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.49  E-value: 2.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 626
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 627 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIAN---DLrcncyTGADLTALVREASLCALRQEi 703
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFIMakdEL-----SGADIKAICTEAGLLALRER- 408
                        250       260
                 ....*....|....*....|....*.
gi 568911103 704 taqkngvgagELKVSHKHFEDAFKKV 729
Cdd:PTZ00361 409 ----------RMKVTQADFRKAKEKV 424
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
180-322 2.48e-45

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: 159.60  E-value: 2.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 180 HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDE 259
Cdd:cd19528   15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDE 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103 260 IDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19528   95 LDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
160-323 2.71e-44

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: 156.90  E-value: 2.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVCKM-LIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA-----APEIVSGVS 233
Cdd:cd19517    1 DIGGLSHYINQLKEMvFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 234 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPA 313
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|
gi 568911103 314 LRRAGRFDRE 323
Cdd:cd19517  158 LRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
178-322 6.30e-43

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: 152.64  E-value: 6.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 178 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 257
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911103 258 DEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19530   96 DEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
476-639 7.19e-43

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: 153.05  E-value: 7.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 550
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 551 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILR 630
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*....
gi 568911103 631 PGRLDKTLF 639
Cdd:cd19517  161 PGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
470-640 3.47e-42

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: 151.17  E-value: 3.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 548
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 549 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-ETRQQVFILAATNRPDIIDPA 627
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 568911103 628 ILRpgRLDKTLFV 640
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
476-640 6.92e-42

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: 149.88  E-value: 6.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLGL-GTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 554
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 555 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpg 632
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAILR-- 158

                 ....*...
gi 568911103 633 RLDKTLFV 640
Cdd:cd19520  159 RMPKRFHI 166
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
179-324 3.27e-41

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: 147.96  E-value: 3.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 179 RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFID 258
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103 259 EIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 324
Cdd:cd19526   94 EFDSIAPKRGHDSTGVTDRVVNQLLTQLD---GVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
161-324 4.87e-39

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: 142.11  E-value: 4.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 161 VGGND---ATLKEVckMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 237
Cdd:cd19509    1 IAGLDdakEALKEA--VILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 238 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRa 317
Cdd:cd19509   78 KIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN-KPEDRVLVLGATNRPWELDEAFLR- 155

                 ....*..
gi 568911103 318 gRFDREV 324
Cdd:cd19509  156 -RFEKRI 161
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
476-640 8.41e-39

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: 141.66  E-value: 8.41e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 554
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 555 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------ETRQQVFILAATNRPDIIDP 626
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 568911103 627 AILRpgRLDKTLFV 640
Cdd:cd19522  159 ALRR--RLEKRIYI 170
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
178-322 2.41e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 136.87  E-value: 2.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 178 MRHPEVYQhLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 257
Cdd:cd19527   13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103 258 DEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19527   92 DELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPDLLDPALLRPGRFDK 156
cell_div_CdvC NF041006
cell division protein CdvC;
155-380 4.38e-37

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.95  E-value: 4.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 155 NVKFEDVGG-NDAtlKEVCKMLI--HMRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSG 231
Cdd:NF041006  99 KVTFSDIVGlEDV--KEALKEAIvyPSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 232 VSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGAT 304
Cdd:NF041006 174 WLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGAT 250
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103 305 NRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 380
Cdd:NF041006 251 NKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
470-640 8.58e-37

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: 136.66  E-value: 8.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 470 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 549
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 550 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPA 627
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 568911103 628 ILRpgRLDKTLFV 640
Cdd:cd19525  176 ARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
477-635 1.87e-35

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: 132.23  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 477 IGALE-DIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYV 550
Cdd:cd19504    2 IGGLDkEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 551 GESERAVRQVF------QRAK--NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLETRQQVFILAATNR 620
Cdd:cd19504   78 GESEANIRKLFadaeeeQRRLgaNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNR 157
                        170
                 ....*....|....*
gi 568911103 621 PDIIDPAILRPGRLD 635
Cdd:cd19504  158 KDLIDEALLRPGRLE 172
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
155-338 2.26e-35

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.00  E-value: 2.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  155 NVKFEDVGGNDATLKevckmLIH------MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPI-------- 220
Cdd:TIGR03689 178 DVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIgaegggks 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  221 --LKVAAPEIVSGVSGESEQKLRELFDQAVSNA----PCIVFIDEIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVA 293
Cdd:TIGR03689 253 yfLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568911103  294 ATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERIL 338
Cdd:TIGR03689 330 SLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
476-640 3.01e-34

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: 128.43  E-value: 3.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTPA-GILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 554
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 555 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpg 632
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 568911103 633 RLDKTLFV 640
Cdd:cd19524  157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
155-324 3.40e-32

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: 122.66  E-value: 3.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 155 NVKFEDVGGNDATlKEVCK--MLIHMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 232
Cdd:cd19521    3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 233 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDP 312
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGN--DSQGVLVLGATNIPWQLDS 158
                        170
                 ....*....|..
gi 568911103 313 ALRRagRFDREV 324
Cdd:cd19521  159 AIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
160-316 8.08e-31

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: 118.68  E-value: 8.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGND---ATLKEvcKMLIHMRHPEVYQHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 235
Cdd:cd19520    1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 236 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALR 315
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLST-DGNCRVIVMGATNRPQDLDEAIL 157

                 .
gi 568911103 316 R 316
Cdd:cd19520  158 R 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
156-316 7.34e-30

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: 116.63  E-value: 7.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 156 VKFEDVGGND---ATLKEVckMLIHMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 232
Cdd:cd19525   19 INWADIAGLEfakKTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 233 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLnNVAATARVLVIGATNRPDSLDP 312
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGA-TTSSEDRILVVGATNRPQEIDE 174

                 ....
gi 568911103 313 ALRR 316
Cdd:cd19525  175 AARR 178
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
476-640 9.68e-30

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: 115.54  E-value: 9.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELimailaPVRNP---DQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 552
Cdd:cd19507    1 DVGGLDNLKDWL------KKRKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 553 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAATNRPDIIDPAILRP 631
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*....
gi 568911103 632 GRLDKTLFV 640
Cdd:cd19507  153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
506-642 9.69e-29

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 112.24  E-value: 9.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 506 LGTPAGILLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFDEVDA 579
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103 580 LCPRrsdretgASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGL 642
Cdd:cd00009   96 LSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
188-322 4.27e-28

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: 110.54  E-value: 4.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 188 GVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPK 266
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103 267 REVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19507  107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
166-316 2.71e-27

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: 108.92  E-value: 2.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 166 ATLKEVCKML-----IHMRHPEVYQhlGVVPP-RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQK 239
Cdd:cd19522    3 ADLEEAKKLLeeavvLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 240 LRELFDQAVSNAPCIVFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPAL 314
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEAL 160

                 ..
gi 568911103 315 RR 316
Cdd:cd19522  161 RR 162
ycf46 CHL00195
Ycf46; Provisional
154-368 5.12e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 115.50  E-value: 5.12e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 154 SNVKFEDVGGNDatlkeVCKMLIHMRH---PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVS 230
Cdd:CHL00195 223 VNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 231 GVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDS 309
Cdd:CHL00195 298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911103 310 LDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRlP---ETFNFCHLAHLTPGFVGADL 368
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIKKLSKLSNKFSGAEI 433
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
191-327 1.16e-26

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 106.46  E-value: 1.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 191 PPRGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSGVSGESEQK---LRELFDQAVSNAPCIVFIDEIDAIT 264
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDSLS 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911103 265 pkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGRFDREVCLG 327
Cdd:cd00009   98 -----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
160-316 1.21e-26

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: 106.86  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGNDATLKEVCKMLI-HMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 238
Cdd:cd19524    1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 239 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPA-LRR 316
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS-NGDDRVLVMGATNRPQELDDAvLRR 157
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
161-324 1.19e-25

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: 104.11  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 161 VGGNDATLKEVCKMLIHMR--HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK-VAAPEIVSGVSGESE 237
Cdd:cd19504    2 IGGLDKEFSDIFRRAFASRvfPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 238 QKLRELFDQA---------VSNAPCIVFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNvaatarVLVIGA 303
Cdd:cd19504   82 ANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNN------ILVIGM 154
                        170       180
                 ....*....|....*....|.
gi 568911103 304 TNRPDSLDPALRRAGRFDREV 324
Cdd:cd19504  155 TNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
415-694 4.98e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 109.34  E-value: 4.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 415 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVALAEVQPSA-------KRE--------GFV 467
Cdd:CHL00195 144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATYKTIDENSiplileeKKQiisqteilEFY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 468 TVpNVTWADIGALEDIRDELimailapvrnpdQFRT---------LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFI 538
Cdd:CHL00195 222 SV-NEKISDIGGLDNLKDWL------------KKRStsfskqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 539 SVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAA 617
Cdd:CHL00195 289 RLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVAT 366
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103 618 TNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKtITKNGTKPPLDEDVNLETIAndLRCNCYTGADLTALVREA 694
Cdd:CHL00195 367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFK-IHLQKFRPKSWKKYDIKKLS--KLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
476-640 4.11e-20

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: 88.02  E-value: 4.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 476 DIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 555
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 556 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpgR 633
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGsgEDGVLVVCTTSKPEEIDESLRR--Y 156

                 ....*..
gi 568911103 634 LDKTLFV 640
Cdd:cd19523  157 FSKRLLV 163
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
160-316 2.38e-19

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: 85.71  E-value: 2.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 160 DVGGND---ATLKEvcKMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 236
Cdd:cd19523    1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 237 EQKLRELFDQAVSNAPCIVFIDEIDAITPKReVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRR 316
Cdd:cd19523   78 EKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLG-SGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
508-643 1.09e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.19  E-value: 1.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103   508 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 570
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103   571 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 643
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
191-330 1.21e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.19  E-value: 1.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103   191 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFDQAVSNAPC 253
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103   254 IVFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREVCLGIPD 330
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
178-324 2.92e-18

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: 82.40  E-value: 2.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 178 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESEQKLRELfdqavSNAP--CIV 255
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLL-----NTAPkqSII 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911103 256 FIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 324
Cdd:cd19510   80 LLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALD---GVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
512-627 2.03e-13

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: 69.78  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 576
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568911103 577 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPA 627
Cdd:cd19508  134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
495-635 3.28e-12

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 65.07  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 495 VRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 573
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911103 574 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 635
Cdd:cd19510   81 LEDIDAAFESREHNkknpsAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVD 148
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
512-628 9.40e-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: 63.31  E-value: 9.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 590
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568911103 591 ASVR-VVNQLLTEMdGLETRQQVFILaATNRPDIIDPAI 628
Cdd:cd19512  104 EDLRaALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 140
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
193-324 1.01e-10

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 60.62  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIA--GELDLPILKVA--APEIVSGVSgeseqKLRELFDQA-VSNAPCIVFIDEIDAITPKR 267
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGdvAPMGREGVT-----AIHKVFDWAnTSRRGLLLFVDEADAFLRKR 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 268 --EVASKDMeRRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRraGRFDREV 324
Cdd:cd19512   98 stEKISEDL-RAALNAFLYRTGEQSN-----KFMLVLASNQPEQFDWAIN--DRIDEMV 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
195-260 1.45e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.95  E-value: 1.45e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVsgeseQKLRELFDQAVSNA----PCIVFIDEI 260
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA--VTSGV-----KDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
504-636 1.82e-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: 60.08  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 504 LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 569
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911103 570 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLETRQQVFIlAATNRPDIIDPAILRPGRLDK 636
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
195-260 1.85e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.85e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVSgeseqKLRELFDQA----VSNAPCIVFIDEI 260
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGVK-----DIREVIEEArerrAYGRRTILFVDEI 114
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
193-314 4.84e-10

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: 59.77  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIAGELDL---------PILKVAAPEIVSGVSGESEQKLRELFDQA---VSNAPCIVF--ID 258
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKDALVFvlID 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 259 EIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 314
Cdd:cd19508  133 EVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKR---YHNNVILLTSNLLEKIDVAF 189
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
186-322 1.27e-09

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 57.77  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 186 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA--------------APEIVSGVSGESEQKLRELFDQAVSNA 251
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568911103 252 PCIVFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDR 322
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
157-266 2.58e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 60.32  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 157 KFEDVGGNDATLKEVCKMLihmrhpEVYQHlgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP-----EIVSG 231
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI------ESWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIER 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568911103 232 VSGESEQKlRELFDQAVSnapcIVFIDEIDAITPK 266
Cdd:PRK04195  84 VAGEAATS-GSLFGARRK----LILLDEVDGIHGN 113
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
351-384 9.14e-09

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: 51.77  E-value: 9.14e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568911103  351 FNFCHLAHLTPGFVGADLMALCREAAMCAVNRVL 384
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGL 35
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
667-724 3.23e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 50.23  E-value: 3.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568911103  667 DVNLETIANdlRCNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFED 724
Cdd:pfam17862   1 DVDLEELAE--RTEGFSGADLEALCREAALAALRRGLEA-----------VTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
190-320 6.01e-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: 53.15  E-value: 6.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 190 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEI--VSGVSGESEQKLRELFDQavsnapcIVFIDEIDAITPKR 267
Cdd:cd19498   44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVEG-------IVFIDEIDKIAKRG 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103 268 EVASKDMERRIVAQLL------TCMDDLNNVAATARVLVIGA----TNRPDSLDPALRraGRF 320
Cdd:cd19498  117 GSSGPDVSREGVQRDLlpivegSTVSTKYGPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
195-376 1.37e-07

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: 53.63  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAA-----PEIVSGVS------GESEQKLRELFDQavsnapcIVFIDEIDAI 263
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllPSDILGTYiydqqtGEFEFRPGPLFAN-------VLLADEINRA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 264 TPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS-----LDPALRRagRFDREVCLGIPDEA 332
Cdd:COG0714  107 PPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPDAE 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568911103 333 ARERILqtlcrKLRLPEtfnfcHLAHLTPGFVGADLMALCREAA 376
Cdd:COG0714  174 EEREIL-----RRHTGR-----HLAEVEPVLSPEELLALQELVR 207
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
194-320 4.05e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  194 GVLLHGPPGCGKTLLAHAIAGELD-LPILKVAAP------EIVSGVsgESEQKLRELFDQAVSNA---PCIVFIDEIDAI 263
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRR--NIDPGGASWVDGPLVRAareGEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  264 TPKrevaskdmerrIVAQLLTCMDD----LNN-----VAATARVLVIGATNRPD----SLDPALRRagRF 320
Cdd:pfam07728  79 NPD-----------VLNSLLSLLDErrllLPDggelvKAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
512-582 5.86e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 5.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 577
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                         90
                 ....*....|
gi 568911103 578 -----DALCP 582
Cdd:PRK13342 105 nkaqqDALLP 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
512-614 6.38e-07

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 52.92  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  512 ILLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRR 584
Cdd:TIGR03922 315 MLFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
                          90       100       110
                  ....*....|....*....|....*....|
gi 568911103  585 SDRETGASVRVVNQLLTEMDGLETRQQVFI 614
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARMENDRDRLVVIG 421
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
507-582 8.65e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.98  E-value: 8.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 507 GTPAGILLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFD 575
Cdd:COG2256   47 GRLSSMILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVD 112
                         90
                 ....*....|....*
gi 568911103 576 EV--------DALCP 582
Cdd:COG2256  113 EIhrfnkaqqDALLP 127
PRK04195 PRK04195
replication factor C large subunit; Provisional
512-678 1.26e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 51.46  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 583
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 584 RSDReTGAS--VRVVNqlltemdglETRQQVfILAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--VAILKTITKN- 658
Cdd:PRK04195 113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                        170       180
                 ....*....|....*....|....
gi 568911103 659 GTKppLDEDVnLETIAN----DLR 678
Cdd:PRK04195 177 GIE--CDDEA-LKEIAErsggDLR 197
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
193-251 3.09e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.35  E-value: 3.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSgvsgeSEQKLRELFDQAVSNA 251
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYS-----AELKKTEFLMQALRKA 120
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
195-268 9.99e-06

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: 47.59  E-value: 9.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV-SGVSGES-EQKLRELFDQA---VSNAP-CIVFIDEIDAITPKRE 268
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLLQAAdydVERAQrGIVYIDEIDKIARKSE 132
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
195-320 1.06e-05

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: 46.34  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDQAVSNAPC-IVFIDEIDAITPK-REVASK 272
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLAAILTNLEPGdVLFIDEIHRLNRAvEEILYP 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103  273 DMERRivaqlltCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 320
Cdd:pfam05496 107 AMEDF-------RLDIVIGKGPSARSIrldlppftLVGATTRAGLLTSPLR--DRF 153
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
193-324 1.19e-05

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: 48.69  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  193 RGVLLHGPPGCGKTLLAHAIA------GELDLP-ILKVAAPEIVSGVSGESEQKLRELFDQAVSNapcIVFIDEIDAITP 265
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568911103  266 KREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPD-----SLDPALRRagRFDREV 324
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMENDRD-----RLVVIGAGYRKDldkflEVNEGLRS--RFTRVI 446
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
484-674 1.60e-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: 47.47  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 484 RDELIMAILApvrnpdqfrTLGLGTPagILLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESE 554
Cdd:COG0714   17 QEELIELVLI---------ALLAGGH--LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 555 RAVRQ--VFQRaknsapcVIFFDEVDalcprRSDRETGASvrvvnqLLTEMD------GLETR---QQVFILAATNRPDI 623
Cdd:COG0714   86 FEFRPgpLFAN-------VLLADEIN-----RAPPKTQSA------LLEAMEerqvtiPGGTYklpEPFLVIATQNPIEQ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103 624 ID-----PAILRpgRLDKTLFVGLPPPADRVAILKTiTKNGTKPPLDEDVNLETIA 674
Cdd:COG0714  148 EGtyplpEAQLD--RFLLKLYIGYPDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
512-545 3.89e-05

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: 44.41  E-value: 3.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568911103  512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 545
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
512-582 4.04e-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: 44.49  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  512 ILLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 573
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 568911103  574 FDEVDALCP 582
Cdd:pfam07724  81 IDEIEKAHP 89
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
192-315 4.06e-05

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.12  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 192 PRGVLLHGPPGCGKTLLAHAIAGEL-------DLPILKVAAPEIVSGVSGEseqkLRELFDQAVSNApcIVfIDEIDAIT 264
Cdd:COG0470   18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGNHPD----LLELNPEEKSDQ--IG-IDQIRELG 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568911103 265 PKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPALR 315
Cdd:COG0470   91 EFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTIR 149
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
193-237 5.44e-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: 46.15  E-value: 5.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568911103  193 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSGVSGESE 237
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTE 97
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
512-545 6.80e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 6.80e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 545
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
195-320 6.91e-05

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: 45.37  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDqAVSN--APCIVFIDEIDAITPK-REVAS 271
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAA-ILTNleEGDVLFIDEIHRLSPAvEELLY 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568911103  272 KDMERrivaqllTCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 320
Cdd:TIGR00635 103 PAMED-------FRLDIVIGKGPSARSVrldlppftLVGATTRAGMLTSPLR--DRF 150
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
511-564 8.22e-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: 45.38  E-value: 8.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103  511 GILLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 564
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
193-311 9.00e-05

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: 43.67  E-value: 9.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES--EQKLRELFDQAVSNAPCIVFIDEIDAI----TPK 266
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPK 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568911103 267 REvasKDMERRIVAQLLTCMddLNNVAATARVLVIGATNRPDSLD 311
Cdd:cd19506  107 TE---KQLDPKRLKKDLPKI--LKSLKPEDRVLIVGTTSRPFEAD 146
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
195-265 1.01e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.12  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELF---------DqavsnapcIVFIDEIDAITP 265
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKPGDLAailtnleegD--------VLFIDEIHRLSP 116
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
509-578 1.19e-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: 43.32  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 509 PAGILLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIF 573
Cdd:cd19499   41 IGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVL 118

                 ....*
gi 568911103 574 FDEVD 578
Cdd:cd19499  119 LDEIE 123
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
511-630 1.38e-04

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: 42.28  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  511 GILLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 578
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568911103  579 alcprRSDRETgasVRVVNQLLTE-----MDGLETRQ----QVFILAATNRPDI----IDPAILR 630
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
511-558 1.87e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 1.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568911103 511 GILLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 558
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
195-220 1.89e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 44.30  E-value: 1.89e-04
                         10        20
                 ....*....|....*....|....*.
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGELDLPI 220
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
446-583 2.06e-04

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 42.75  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 446 ELNDFIVAlaevQPSAKREGFVTVPNvTWADIGALEDIRDELimailapvrnpdqfrtlglgTPAGILLAGPPGCGKTLL 525
Cdd:cd19498    8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDEV--------------------TPKNILMIGPTGVGKTEI 62
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103 526 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 583
Cdd:cd19498   63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
512-621 2.46e-04

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: 42.13  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQVFQRAKNSAPCVIFFDEVDALCPR---RSD 586
Cdd:cd19506   29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKkvpKTE 108
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568911103 587 RETGASvRVVNQLLTEMDGLETRQQVFILAATNRP 621
Cdd:cd19506  109 KQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
PRK08116 PRK08116
hypothetical protein; Validated
193-262 3.54e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.09  E-value: 3.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVS---GVSGESEQKLRELFDQAVSNAPCIVfIDEIDA 262
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANELiekGVPVIFVNFPQLLNrikSTYKSSGKEDENEIIRSLVNADLLI-LDDLGA 189
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
473-545 3.88e-04

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: 43.06  E-value: 3.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568911103  473 TWADIGALEDIRDELIMAILAPVRNPDQfrtlglgtPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 545
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
195-255 4.18e-04

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 40.28  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  195 VLLHGPPGCGKTLLAHAIAGELdLPILKVAAPEIVSGVSGE--------------------SEQKLRELFDQAVSNAPCI 254
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSVYSRNPDDdfwdgytgqpvviiddfgqnPDGPDEAELIRLVSSTPYP 79

                  .
gi 568911103  255 V 255
Cdd:pfam00910  80 P 80
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
195-311 4.81e-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: 40.56  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 195 VLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVsgvsgeseqkLRELFDQAVSNAPCIVFIDEIDAITPKREVAS 271
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568911103 272 KDMERRIVAQLLtcmddlnNVAATARVLVIgATNRPDSLD 311
Cdd:cd01120   71 SSELLEDLAKLL-------RAARNTGITVI-ATIHSDKFD 102
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
512-543 5.66e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.76  E-value: 5.66e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFISVKGP 543
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
484-615 7.86e-04

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: 40.95  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  484 RDELIMAILapvrnpDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV---ANESGLNFISVKGPELLNMYVG----ESERA 556
Cdd:pfam13191   5 REEELEQLL------DALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568911103  557 VRQVFQRAKNSAPcVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFIL 615
Cdd:pfam13191  79 LRQLLDELESSLL-EAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
196-264 8.44e-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: 41.00  E-value: 8.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 196 LLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESE-----------------QKLRelfdQAVSNAPCIVfID 258
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirghrrtyvgampgriiQALK----KAGTNNPVFL-LD 111

                 ....*.
gi 568911103 259 EIDAIT 264
Cdd:cd19500  112 EIDKIG 117
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
195-265 1.19e-03

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: 40.26  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103  195 VLLHGPPGCGKTLLAHAIAGELD-----LPI--------------LKVAAPEIVSgvSGESEQklreLFDQAVSNAPCIV 255
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgderaLIRidmseymeehsvsrLIGAPPGYVG--YEEGGQ----LTEAVRRKPYSIV 79
                          90
                  ....*....|
gi 568911103  256 FIDEIDAITP 265
Cdd:pfam07724  80 LIDEIEKAHP 89
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
512-580 1.68e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 40.23  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 580
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
193-271 4.54e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 193 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSG-VSGESEQKLRELFDQaVSNAPCIVfIDEIDAITPKRE 268
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNElKEARADGRLERLLKR-LAKVDLLI-LDELGYLPLDAE 177

                 ...
gi 568911103 269 VAS 271
Cdd:COG1484  178 GAE 180
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
512-539 5.32e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 38.24  E-value: 5.32e-03
                         10        20
                 ....*....|....*....|....*...
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFIS 539
Cdd:cd02020    2 IAIDGPAGSGKSTVAKLLAKKLGLPYLD 29
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
512-539 5.75e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 38.56  E-value: 5.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 568911103  512 ILLAGPPGCGKTLLAKAVANESGLNFIS 539
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLIS 30
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
192-346 6.46e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 192 PRG--VLLHGPPGCGKTLLAHAIAGELdlpilkVAAPE---IVSgvSGESEQKLREL-------FDQAVSNApCIVFIDe 259
Cdd:COG0467   18 PRGssTLLSGPPGTGKTTLALQFLAEG------LRRGEkglYVS--FEESPEQLLRRaeslgldLEEYIESG-LLRIID- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568911103 260 idaITPKREVASKDMerrIVAQLLTCMDDLNnvaatARVLVIgatnrpDSLDpALRRAgrfdrevclgIPDEAARERILQ 339
Cdd:COG0467   88 ---LSPEELGLDLEE---LLARLREAVEEFG-----AKRVVI------DSLS-GLLLA----------LPDPERLREFLH 139

                 ....*..
gi 568911103 340 TLCRKLR 346
Cdd:COG0467  140 RLLRYLK 146
PRK04182 PRK04182
cytidylate kinase; Provisional
512-539 6.48e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 38.25  E-value: 6.48e-03
                         10        20
                 ....*....|....*....|....*...
gi 568911103 512 ILLAGPPGCGKTLLAKAVANESGLNFIS 539
Cdd:PRK04182   3 ITISGPPGSGKTTVARLLAEKLGLKHVS 30
PRK13764 PRK13764
ATPase; Provisional
511-531 7.53e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 39.82  E-value: 7.53e-03
                         10        20
                 ....*....|....*....|.
gi 568911103 511 GILLAGPPGCGKTLLAKAVAN 531
Cdd:PRK13764 259 GILIAGAPGAGKSTFAQALAE 279
 
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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