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Conserved domains on  [gi|32699478|sp|Q9DBY8|]
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RecName: Full=Nuclear valosin-containing protein-like; Short=NVLp; Short=Nuclear VCP-like protein

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 13875340)

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 ...
242-855 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: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   242 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 320
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   321 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 400
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   401 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 480
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   481 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 560
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   561 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 640
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   641 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 719
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   720 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 799
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478   800 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 855
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 1.90e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


:

Pssm-ID: 465247  Cd Length: 70  Bit Score: 114.26  E-value: 1.90e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32699478     2 KPRPGVFVDRKLKQRVIQYLSSNRCGKYVDTGILASDLQRLYSvDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
242-855 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: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   242 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 320
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   321 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 400
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   401 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 480
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   481 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 560
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   561 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 640
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   641 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 719
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   720 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 799
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478   800 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 855
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 ...
265-431 6.45e-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: 328.59  E-value: 6.45e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 343
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 344 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 422
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                ....*....
gi 32699478 423 GRFDREVCL 431
Cdd:cd19518 161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
506-839 6.07e-106

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: 6.07e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 506 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 585
Cdd:COG1222   8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 586 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 665
Cdd:COG1222  84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 666 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:COG1222 164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 745 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 824
Cdd:COG1222 244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                       330
                ....*....|....*
gi 32699478 825 KHFEDAFKKVKPSIS 839
Cdd:COG1222 308 EDLEKAIEKVKKKTE 322
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
552-846 2.44e-77

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.30  E-value: 2.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  552 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 625
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  626 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 702
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  703 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 781
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478  782 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 846
Cdd:PRK03992 333 T--EGASGADLKAICTEAGMFAIRDDRTE-----------VTMEDFLKAIEKVmgkeEKDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
617-747 3.80e-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: 188.96  E-value: 3.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 696
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 32699478   697 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 747
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
575-848 7.66e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.93  E-value: 7.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  655 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 726
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  727 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 806
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 32699478  807 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 848
Cdd:NF041006 327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
cell_div_CdvC NF041006
cell division protein CdvC;
260-485 1.72e-36

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 141.80  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  260 NVKFEDVGGndatLKEVCKMLIH-----MRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV 334
Cdd:NF041006  99 KVTFSDIVG----LEDVKEALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIM 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  335 SGVSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIG 407
Cdd:NF041006 172 SKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIG 248
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478  408 ATNRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 485
Cdd:NF041006 249 ATNKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 1.90e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


Pssm-ID: 465247  Cd Length: 70  Bit Score: 114.26  E-value: 1.90e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32699478     2 KPRPGVFVDRKLKQRVIQYLSSNRCGKYVDTGILASDLQRLYSvDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
613-748 9.74e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.58  E-value: 9.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478    613 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 675
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478    676 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 748
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 ...
242-855 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: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   242 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 320
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   321 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 400
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   401 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 480
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   481 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 560
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   561 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 640
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   641 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 719
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   720 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 799
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478   800 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 855
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 ...
265-431 6.45e-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: 328.59  E-value: 6.45e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 343
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 344 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 422
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                ....*....
gi 32699478 423 GRFDREVCL 431
Cdd:cd19518 161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
506-839 6.07e-106

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: 6.07e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 506 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 585
Cdd:COG1222   8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 586 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 665
Cdd:COG1222  84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 666 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:COG1222 164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 745 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 824
Cdd:COG1222 244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                       330
                ....*....|....*
gi 32699478 825 KHFEDAFKKVKPSIS 839
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 ...
585-745 5.12e-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: 310.19  E-value: 5.12e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 585 LEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 664
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 665 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                .
gi 32699478 745 V 745
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 ...
588-745 2.95e-91

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: 284.56  E-value: 2.95e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 588 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 667
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 668 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 745
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
253-485 1.18e-87

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: 1.18e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 253 STELQISNVKFEDVGGNDATLKEVCKMLI-HMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP 331
Cdd:COG1222  67 AVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 332 EIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATN 410
Cdd:COG1222 147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATN 223
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32699478 411 RPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 485
Cdd:COG1222 224 RPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
487-835 2.05e-82

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: 270.24  E-value: 2.05e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 487 RVLMKQQAQQKKKPEIEGLPSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSA 566
Cdd:COG0464  64 ALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 567 KREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVK 646
Cdd:COG0464 144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 647 GPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLetRQQVFILAATNRP 726
Cdd:COG0464 224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRP 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 727 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 806
Cdd:COG0464 302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL 374
                       330       340
                ....*....|....*....|....*....
gi 32699478 807 eitaqkngvgaGELKVSHKHFEDAFKKVK 835
Cdd:COG0464 375 -----------GREPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
552-846 2.44e-77

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.30  E-value: 2.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  552 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 625
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  626 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 702
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  703 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 781
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478  782 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 846
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 ...
265-431 7.70e-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: 243.74  E-value: 7.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 342
Cdd:cd19503   1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 343 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRA 422
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS---RGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 32699478 423 GRFDREVCL 431
Cdd:cd19503 157 GRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
263-485 1.27e-71

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: 240.97  E-value: 1.27e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 263 FEDVGGNDATLKEVCKMLIHMRH-PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 341
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 342 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRR 421
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRS-----DVVVIAATNRPDLLDPALLR 310
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32699478 422 agRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 485
Cdd:COG0464 311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
588-745 9.04e-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: 227.38  E-value: 9.04e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 588 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 667
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 668 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 745
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 ...
588-745 6.14e-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: 225.08  E-value: 6.14e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 588 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 667
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 668 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 32699478 745 V 745
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 ...
581-741 1.06e-67

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: 222.17  E-value: 1.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 660
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 661 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 740
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                .
gi 32699478 741 K 741
Cdd:cd19503 161 R 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
575-834 1.41e-66

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: 1.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   575 PNVTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   655 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRP 726
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   727 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 806
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVAR--RTPGFSGADLANLLNEAALLAARK 278
                         250       260
                  ....*....|....*....|....*...
gi 32699478   807 EITAqkngvgagelkVSHKHFEDAFKKV 834
Cdd:TIGR01241 279 NKTE-----------ITMNDIEEAIDRV 295
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
588-744 3.70e-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: 217.68  E-value: 3.70e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 588 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 667
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32699478 668 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
265-432 3.99e-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: 3.99e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 343
Cdd:cd19519   1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 344 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAG 423
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK---QRAHVIVMAATNRPNSIDPALRRFG 157

                ....*....
gi 32699478 424 RFDREVCLG 432
Cdd:cd19519 158 RFDREIDIG 166
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
247-485 4.95e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 220.09  E-value: 4.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  247 KKAKARSTELQIS-NVKFEDVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDL 323
Cdd:PRK03992 113 KDPRVQAMEVIESpNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNA 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  324 PILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaT 400
Cdd:PRK03992 192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---R 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  401 ARVLVIGATNRPDSLDPALRRAGRFDR--EVCLgiPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCR 478
Cdd:PRK03992 269 GNVKIIAATNRIDILDPAILRPGRFDRiiEVPL--PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICT 346

                 ....*..
gi 32699478  479 EAAMCAV 485
Cdd:PRK03992 347 EAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
248-487 1.88e-63

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: 1.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   248 KAKARSTELQISNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 327
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   328 VAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKRE---VASKDMERRIVAQLLTCMDDLNNvaaTARVL 404
Cdd:TIGR01241 119 ISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT---NTGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   405 VIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCA 484
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275

                  ...
gi 32699478   485 VNR 487
Cdd:TIGR01241 276 ARK 278
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
584-745 6.34e-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: 205.98  E-value: 6.34e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 584 ALEDIRDelimaILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 663
Cdd:cd19481   1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 664 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKT 742
Cdd:cd19481  76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                ...
gi 32699478 743 LFV 745
Cdd:cd19481 156 IEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
575-834 2.07e-61

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 218.37  E-value: 2.07e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 575 PNVTWADI-GA------LEDIRDELimailapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKG 647
Cdd:COG0465 137 PKVTFDDVaGVdeakeeLQEIVDFL--------KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 648 PELLNMYVG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLETRQQV 717
Cdd:COG0465 209 SDFVEMFVGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGV 281
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 718 FILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtKpPLDEDVNLETIANdlRCNCYTGADLTALVR 797
Cdd:COG0465 282 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIAR--RTPGFSGADLANLVN 356
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 32699478 798 EASLCALRqeitaqkngvgAGELKVSHKHFEDAFKKV 834
Cdd:COG0465 357 EAALLAAR-----------RNKKAVTMEDFEEAIDRV 382
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
248-487 1.12e-59

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 213.36  E-value: 1.12e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 248 KAKARSTELQISNVKFEDVGGND---ATLKEVCKMLihmRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLP 324
Cdd:COG0465 126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 325 ILKVAAPEIVS---GVsGESeqKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDmER-RIVAQLLTCMD--Dln 395
Cdd:COG0465 203 FFSISGSDFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGHD-EReQTLNQLLVEMDgfE-- 276
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 396 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 475
Cdd:COG0465 277 ---GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353
                       250
                ....*....|..
gi 32699478 476 LCREAAMCAVNR 487
Cdd:COG0465 354 LVNEAALLAARR 365
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
588-745 1.61e-59

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: 199.66  E-value: 1.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 588 IRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 667
Cdd:cd19527   1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 668 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-TRQQVFILAATNRPDIIDPAILRPGRLDKTLF 744
Cdd:cd19527  80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                .
gi 32699478 745 V 745
Cdd:cd19527 160 L 160
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
578-741 2.02e-59

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: 199.87  E-value: 2.02e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 578 TWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 657
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 658 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAIL 734
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                ....*..
gi 32699478 735 RPGRLDK 741
Cdd:cd19502 161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
577-834 5.99e-59

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 212.60  E-value: 5.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  577 VTWADIGALEDIRDEL--IMAILapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFeeVVSFL---KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  655 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLETRQQVFILAATNRP 726
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRV 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  727 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 806
Cdd:CHL00176 332 DILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARR 406
                        250       260
                 ....*....|....*....|....*...
gi 32699478  807 EITaqkngvgagelKVSHKHFEDAFKKV 834
Cdd:CHL00176 407 KKA-----------TITMKEIDTAIDRV 423
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
577-745 2.26e-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: 196.68  E-value: 2.26e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 577 VTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 656
Cdd:cd19501   1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 657 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAI 733
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 32699478 734 LRPGRLDKTLFV 745
Cdd:cd19501 160 LRPGRFDRQVYV 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
263-480 3.47e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 196.26  E-value: 3.47e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 263 FEDVGGNDATlKEVCKMLIH-MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 341
Cdd:COG1223   1 LDDVVGQEEA-KKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 342 EQKLRELFDQAvSNAPCIVFIDEIDAITPKREVASKDME-RRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALR 420
Cdd:COG1223  80 ARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDGLPS-----GSVVIAATNHPELLDSALW 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 421 RagRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 480
Cdd:COG1223 154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
532-772 5.13e-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: 5.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   532 GLLRDQDPLSEEQMQGLCIELndfiVALAEVQPSAKREgfvtVPNVTWADIGAL----EDIRDelimAILAPVRNPDQFR 607
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEA----IPRTEVEDLVLEE----VPDVTYADIGGLgsqiEQIRD----AVELPFLHPELYR 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   608 TLGLGTPAGILLAGPPGCGKTLLAKAVAN-------ESGLN---FISVKGPELLNMYVGESERAVRQVFQRAKNSA---- 673
Cdd:TIGR03689 210 EYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegr 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   674 PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLP 748
Cdd:TIGR03689 290 PVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERP 365
                         250       260
                  ....*....|....*....|....*
gi 32699478   749 PPADRVAIL-KTITKNgtkPPLDED 772
Cdd:TIGR03689 366 DAEAAADIFaKYLTDD---LPLPED 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
617-747 3.80e-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: 188.96  E-value: 3.80e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 696
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 32699478   697 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 747
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
581-746 1.08e-55

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: 1.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 660
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 661 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 740
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                ....*.
gi 32699478 741 KTLFVG 746
Cdd:cd19519 161 REIDIG 166
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
575-834 1.78e-55

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 196.91  E-value: 1.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  655 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 731
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  732 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRqeitaq 811
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAICQEAGMQAVR------ 368
                        250       260
                 ....*....|....*....|...
gi 32699478  812 KNgvgagELKVSHKHFEDAFKKV 834
Cdd:PTZ00454 369 KN-----RYVILPKDFEKGYKTV 386
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
282-429 9.78e-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: 186.33  E-value: 9.78e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 282 HMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVF 361
Cdd:cd19481  12 PRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILF 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 362 IDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREV 429
Cdd:cd19481  91 IDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
578-852 6.75e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 198.33  E-value: 6.75e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  578 TWADIGALEDIRDElIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 657
Cdd:PRK10733 150 TFADVAGCDEAKEE-VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  658 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLETRQQVFILAATNRPDII 729
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  730 DPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDlrCNCYTGADLTALVREASLCALRqeit 809
Cdd:PRK10733 304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 32699478  810 aqkngvgAGELKVSHKHFEDAFKKVKPSISIKDQVMYEALQRS 852
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 ...
273-427 7.10e-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: 184.02  E-value: 7.10e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 273 LKEVCKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFD 350
Cdd:cd19511   1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32699478 351 QAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
248-484 4.40e-53

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 196.02  E-value: 4.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  248 KAKARS-TELQISNVkFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPIL 326
Cdd:PRK10733 136 KSKARMlTEDQIKTT-FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  327 KVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREV---ASKDMERRIVAQLLTCMDDLNnvaATARV 403
Cdd:PRK10733 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE---GNEGI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  404 LVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMC 483
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371

                 .
gi 32699478  484 A 484
Cdd:PRK10733 372 A 372
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
300-432 3.67e-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: 178.17  E-value: 3.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDM 379
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 32699478   380 ERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREVCLG 432
Cdd:pfam00004  81 SRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
261-429 9.11e-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: 178.58  E-value: 9.11e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 261 VKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 340
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 341 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDMERRIVAQLLTCMDDLnnvAATARVLVIGATNRPDSLDP 417
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGF---ESNTGVIVIAATNRPDVLDP 157
                       170
                ....*....|..
gi 32699478 418 ALRRAGRFDREV 429
Cdd:cd19501 158 ALLRPGRFDRQV 169
ftsH CHL00176
cell division protein; Validated
239-487 1.03e-51

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.19  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  239 GEIEALLQKKAKarstelqiSNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIA 318
Cdd:CHL00176 166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  319 GELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDMER-RIVAQLLTCMDDLN 395
Cdd:CHL00176 238 GEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEReQTLNQLLTEMDGFK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  396 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 475
Cdd:CHL00176 318 ---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLAN 394
                        250
                 ....*....|..
gi 32699478  476 LCREAAMCAVNR 487
Cdd:CHL00176 395 LLNEAAILTARR 406
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
581-741 1.95e-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: 174.90  E-value: 1.95e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 660
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 661 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----ETRQQVFILAATNRPDIIDPAILRP 736
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                ....*
gi 32699478 737 GRLDK 741
Cdd:cd19518 161 GRFDR 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
596-835 2.01e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.38  E-value: 2.01e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 596 ILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNsAPC 675
Cdd:COG1223  17 IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFARR-APC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 676 VIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLetRQQVFILAATNRPDIIDPAILRpgRLDKTLFVGLPPPADRV 754
Cdd:COG1223  96 VIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 755 AILKtitKNGTKPPLDEDVNLETIANdlRCNCYTGADLTALVREaslcALRQEITAQKNgvgagelKVSHKHFEDAFKKV 834
Cdd:COG1223 172 EILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----ALKKAILEDRE-------KVTKEDLEEALKQR 235

                .
gi 32699478 835 K 835
Cdd:COG1223 236 K 236
cell_div_CdvC NF041006
cell division protein CdvC;
575-848 7.66e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.93  E-value: 7.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  655 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 726
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  727 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 806
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 32699478  807 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 848
Cdd:NF041006 327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
582-745 8.50e-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: 8.50e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 582 IGALEDIRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 661
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 662 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpgRL 739
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                ....*.
gi 32699478 740 DKTLFV 745
Cdd:cd19509 158 EKRIYI 163
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
263-429 4.12e-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: 4.12e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 263 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 341
Cdd:cd19502   2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 342 EQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPA 418
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFD---PRGNIKVIMATNRPDILDPA 158
                       170
                ....*....|.
gi 32699478 419 LRRAGRFDREV 429
Cdd:cd19502 159 LLRPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
260-487 7.16e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 178.03  E-value: 7.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  260 NVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVS 338
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  339 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMER---RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSL 415
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQ---TTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32699478  416 DPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAVNR 487
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
283-429 6.33e-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: 167.29  E-value: 6.33e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 283 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 362
Cdd:cd19529  13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32699478 363 DEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREV 429
Cdd:cd19529  93 DEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDIIDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
263-485 2.20e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 172.26  E-value: 2.20e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  263 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 341
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  342 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 421
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32699478  422 AGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 485
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
575-834 7.61e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 170.72  E-value: 7.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  655 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 731
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  732 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIAN---DLrcncyTGADLTALVREASLCALRQEi 808
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFIMakdEL-----SGADIKAICTEAGLLALRER- 408
                        250       260
                 ....*....|....*....|....*.
gi 32699478  809 taqkngvgagELKVSHKHFEDAFKKV 834
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 ...
285-427 3.28e-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: 3.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 285 HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDE 364
Cdd:cd19528  15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDE 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478 365 IDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19528  95 LDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
265-428 3.75e-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: 157.29  E-value: 3.75e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVCKM-LIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA-----APEIVSGVS 338
Cdd:cd19517   1 DIGGLSHYINQLKEMvFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 339 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPA 418
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALDPA 157
                       170
                ....*....|
gi 32699478 419 LRRAGRFDRE 428
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 ...
283-427 6.22e-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: 153.41  E-value: 6.22e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 283 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 362
Cdd:cd19530  16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32699478 363 DEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19530  96 DEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
581-744 9.37e-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: 9.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 655
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 656 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILR 735
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                ....*....
gi 32699478 736 PGRLDKTLF 744
Cdd:cd19517 161 PGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
575-745 6.40e-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: 150.78  E-value: 6.40e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 653
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 654 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-ETRQQVFILAATNRPDIIDPA 732
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                       170
                ....*....|...
gi 32699478 733 ILRpgRLDKTLFV 745
Cdd:cd19521 160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
581-745 7.38e-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: 150.27  E-value: 7.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLGL-GTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 659
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 660 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpg 737
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAILR-- 158

                ....*...
gi 32699478 738 RLDKTLFV 745
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 ...
284-429 3.39e-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: 148.35  E-value: 3.39e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 284 RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFID 363
Cdd:cd19526  14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478 364 EIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 429
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 ...
266-429 6.15e-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: 6.15e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 266 VGGND---ATLKEVckMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 342
Cdd:cd19509   1 IAGLDdakEALKEA--VILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 343 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRa 422
Cdd:cd19509  78 KIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN-KPEDRVLVLGATNRPWELDEAFLR- 155

                ....*..
gi 32699478 423 gRFDREV 429
Cdd:cd19509 156 -RFEKRI 161
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
581-745 1.12e-38

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: 1.12e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 659
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 660 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------ETRQQVFILAATNRPDIIDP 731
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                       170
                ....*....|....
gi 32699478 732 AILRpgRLDKTLFV 745
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 ...
283-427 2.14e-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: 137.64  E-value: 2.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 283 MRHPEVYQhLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 362
Cdd:cd19527  13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32699478 363 DEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19527  92 DELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
575-745 8.21e-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: 8.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 575 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 654
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 655 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPA 732
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEA 175
                       170
                ....*....|...
gi 32699478 733 ILRpgRLDKTLFV 745
Cdd:cd19525 176 ARR--RLVKRLYI 186
cell_div_CdvC NF041006
cell division protein CdvC;
260-485 1.72e-36

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 141.80  E-value: 1.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  260 NVKFEDVGGndatLKEVCKMLIH-----MRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV 334
Cdd:NF041006  99 KVTFSDIVG----LEDVKEALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIM 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  335 SGVSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIG 407
Cdd:NF041006 172 SKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIG 248
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478  408 ATNRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 485
Cdd:NF041006 249 ATNKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
582-740 2.62e-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: 2.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 582 IGALE-DIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYV 655
Cdd:cd19504   2 IGGLDkEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 656 GESERAVRQVF------QRAK--NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLETRQQVFILAATNR 725
Cdd:cd19504  78 GESEANIRKLFadaeeeQRRLgaNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNR 157
                       170
                ....*....|....*
gi 32699478 726 PDIIDPAILRPGRLD 740
Cdd:cd19504 158 KDLIDEALLRPGRLE 172
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
260-443 2.76e-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: 141.38  E-value: 2.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   260 NVKFEDVGGNDATLKevckmLIH------MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPI-------- 325
Cdd:TIGR03689 178 DVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIgaegggks 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   326 --LKVAAPEIVSGVSGESEQKLRELFDQAVSNA----PCIVFIDEIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVA 398
Cdd:TIGR03689 253 yfLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 32699478   399 ATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERIL 443
Cdd:TIGR03689 330 SLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
581-745 3.43e-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: 3.43e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTPA-GILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 659
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 660 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpg 737
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                ....*...
gi 32699478 738 RLDKTLFV 745
Cdd:cd19524 157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
260-429 4.74e-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: 4.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 260 NVKFEDVGGNDATlKEVCK--MLIHMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 337
Cdd:cd19521   3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 338 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDP 417
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGN--DSQGVLVLGATNIPWQLDS 158
                       170
                ....*....|..
gi 32699478 418 ALRRagRFDREV 429
Cdd:cd19521 159 AIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
265-421 7.70e-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: 119.07  E-value: 7.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGND---ATLKEvcKMLIHMRHPEVYQHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 340
Cdd:cd19520   1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 341 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALR 420
Cdd:cd19520  79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLST-DGNCRVIVMGATNRPQDLDEAIL 157

                .
gi 32699478 421 R 421
Cdd:cd19520 158 R 158
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
2-72 1.90e-30

Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged helix motif. It binds nucleolin.


Pssm-ID: 465247  Cd Length: 70  Bit Score: 114.26  E-value: 1.90e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32699478     2 KPRPGVFVDRKLKQRVIQYLSSNRCGKYVDTGILASDLQRLYSvDYGRRKRNAFRIQVEKVFSIISSEKEL 72
Cdd:pfam16725   1 KKRSGYFSDPRLVPRVEQYLEDNSDSTYVDVDAMADELQRQYR-EYGRRKRNAFRIQVEKAYEIISREYGL 70
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
261-421 6.87e-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: 117.01  E-value: 6.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 261 VKFEDVGGND---ATLKEVckMLIHMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 337
Cdd:cd19525  19 INWADIAGLEfakKTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 338 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLnNVAATARVLVIGATNRPDSLDP 417
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGA-TTSSEDRILVVGATNRPQEIDE 174

                ....
gi 32699478 418 ALRR 421
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 ...
581-745 1.13e-29

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: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELimailaPVRNP---DQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 657
Cdd:cd19507   1 DVGGLDNLKDWL------KKRKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 658 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAATNRPDIIDPAILRP 736
Cdd:cd19507  75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                ....*....
gi 32699478 737 GRLDKTLFV 745
Cdd:cd19507 153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
611-747 1.13e-28

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: 1.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 611 LGTPAGILLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFDEVDA 684
Cdd:cd00009  16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478 685 LCPRrsdretgASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGL 747
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 ...
293-427 4.98e-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: 4.98e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 293 GVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPK 371
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478 372 REVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19507 107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
271-421 3.16e-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: 3.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 271 ATLKEVCKML-----IHMRHPEVYQhlGVVPP-RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQK 344
Cdd:cd19522   3 ADLEEAKKLLeeavvLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 345 LRELFDQAVSNAPCIVFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPAL 419
Cdd:cd19522  81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEAL 160

                ..
gi 32699478 420 RR 421
Cdd:cd19522 161 RR 162
ycf46 CHL00195
Ycf46; Provisional
259-473 1.06e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 114.73  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  259 SNVKFEDVGGNDatlkeVCKMLIHMRH---PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVS 335
Cdd:CHL00195 223 VNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  336 GVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDS 414
Cdd:CHL00195 298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32699478  415 LDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRlP---ETFNFCHLAHLTPGFVGADL 473
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIKKLSKLSNKFSGAEI 433
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
265-421 1.26e-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: 1.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGNDATLKEVCKMLI-HMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 343
Cdd:cd19524   1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 344 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPA-LRR 421
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS-NGDDRVLVMGATNRPQELDDAvLRR 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
296-432 1.36e-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: 1.36e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 296 PPRGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSGVSGESEQK---LRELFDQAVSNAPCIVFIDEIDAIT 369
Cdd:cd00009  18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDSLS 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32699478 370 pkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGRFDREVCLG 432
Cdd:cd00009  98 -----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
266-429 1.54e-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: 1.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 266 VGGNDATLKEVCKMLIHMR--HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK-VAAPEIVSGVSGESE 342
Cdd:cd19504   2 IGGLDKEFSDIFRRAFASRvfPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 343 QKLRELFDQA---------VSNAPCIVFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNvaatarVLVIGA 408
Cdd:cd19504  82 ANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNN------ILVIGM 154
                       170       180
                ....*....|....*....|.
gi 32699478 409 TNRPDSLDPALRRAGRFDREV 429
Cdd:cd19504 155 TNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
520-799 1.11e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 108.57  E-value: 1.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  520 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVALAEVQPSA-------KRE--------GFV 572
Cdd:CHL00195 144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATYKTIDENSiplileeKKQiisqteilEFY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  573 TVpNVTWADIGALEDIRDELimailapvrnpdQFRT---------LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFI 643
Cdd:CHL00195 222 SV-NEKISDIGGLDNLKDWL------------KKRStsfskqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  644 SVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAA 722
Cdd:CHL00195 289 RLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVAT 366
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32699478  723 TNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKtITKNGTKPPLDEDVNLETIAndLRCNCYTGADLTALVREA 799
Cdd:CHL00195 367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFK-IHLQKFRPKSWKKYDIKKLS--KLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
581-745 2.21e-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: 88.79  E-value: 2.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 581 DIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 660
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 661 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpgR 738
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGsgEDGVLVVCTTSKPEEIDESLRR--Y 156

                ....*..
gi 32699478 739 LDKTLFV 745
Cdd:cd19523 157 FSKRLLV 163
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
265-421 1.33e-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: 86.48  E-value: 1.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 265 DVGGND---ATLKEvcKMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 341
Cdd:cd19523   1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 342 EQKLRELFDQAVSNAPCIVFIDEIDAITPKReVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRR 421
Cdd:cd19523  78 EKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLG-SGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
613-748 9.74e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.58  E-value: 9.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478    613 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 675
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478    676 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 748
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
296-435 1.07e-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: 83.58  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478    296 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFDQAVSNAPC 358
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32699478    359 IVFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREVCLGIPD 435
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
283-429 3.76e-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: 82.01  E-value: 3.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 283 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESEQKLRELfdqavSNAP--CIV 360
Cdd:cd19510   9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLL-----NTAPkqSII 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32699478 361 FIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 429
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 ...
617-732 3.07e-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: 69.40  E-value: 3.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 681
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32699478 682 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPA 732
Cdd:cd19508 134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
600-740 4.27e-12

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 64.68  E-value: 4.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 600 VRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 678
Cdd:cd19510   9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32699478 679 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 740
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 ...
617-733 1.14e-11

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: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 695
Cdd:cd19512  25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 32699478 696 ASVR-VVNQLLTEMdGLETRQQVFILaATNRPDIIDPAI 733
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 ...
298-429 1.17e-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: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 298 RGVLLHGPPGCGKTLLAHAIA--GELDLPILKVA--APEIVSGVSgeseqKLRELFDQA-VSNAPCIVFIDEIDAITPKR 372
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGdvAPMGREGVT-----AIHKVFDWAnTSRRGLLLFVDEADAFLRKR 97
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 373 --EVASKDMeRRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRraGRFDREV 429
Cdd:cd19512  98 stEKISEDL-RAALNAFLYRTGEQSN-----KFMLVLASNQPEQFDWAIN--DRIDEMV 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
300-365 1.87e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.95  E-value: 1.87e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVsgeseQKLRELFDQAVSNA----PCIVFIDEI 365
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; ...
609-741 2.05e-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: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 609 LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 674
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32699478 675 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLETRQQVFIlAATNRPDIIDPAILRPGRLDK 741
Cdd:cd19505  87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
300-365 2.29e-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: 2.29e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVSgeseqKLRELFDQA----VSNAPCIVFIDEI 365
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 ...
298-419 7.30e-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: 59.38  E-value: 7.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 298 RGVLLHGPPGCGKTLLAHAIAGELDL---------PILKVAAPEIVSGVSGESEQKLRELFDQA---VSNAPCIVF--ID 363
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKDALVFvlID 132
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 364 EIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 419
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; ...
291-427 1.39e-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: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 291 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA--------------APEIVSGVSGESEQKLRELFDQAVSNA 356
Cdd:cd19505   6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32699478 357 PCIVFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDR 427
Cdd:cd19505  86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
262-371 5.41e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.55  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  262 KFEDVGGNDATLKEVCKMLihmrhpEVYQHlgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP-----EIVSG 336
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI------ESWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIER 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 32699478  337 VSGESEQKlRELFDQAVSnapcIVFIDEIDAITPK 371
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 ...
456-489 1.19e-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: 51.39  E-value: 1.19e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 32699478   456 FNFCHLAHLTPGFVGADLMALCREAAMCAVNRVL 489
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 ...
772-829 4.27e-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: 49.84  E-value: 4.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 32699478   772 DVNLETIANdlRCNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFED 829
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 ...
295-425 7.76e-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: 7.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 295 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEI--VSGVSGESEQKLRELFDQavsnapcIVFIDEIDAITPKR 372
Cdd:cd19498  44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVEG-------IVFIDEIDKIAKRG 116
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478 373 EVASKDMERRIVAQLL------TCMDDLNNVAATARVLVIGA----TNRPDSLDPALRraGRF 425
Cdd:cd19498 117 GSSGPDVSREGVQRDLlpivegSTVSTKYGPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
300-481 1.19e-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: 54.02  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAA-----PEIVSGVS------GESEQKLRELFDQavsnapcIVFIDEIDAI 368
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllPSDILGTYiydqqtGEFEFRPGPLFAN-------VLLADEINRA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 369 TPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS-----LDPALRRagRFDREVCLGIPDEA 437
Cdd:COG0714 107 PPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPDAE 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32699478 438 ARERILqtlcrKLRLPEtfnfcHLAHLTPGFVGADLMALCREAA 481
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 ...
299-425 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: 49.98  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   299 GVLLHGPPGCGKTLLAHAIAGELD-LPILKVAAP------EIVSGVsgESEQKLRELFDQAVSNA---PCIVFIDEIDAI 368
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRR--NIDPGGASWVDGPLVRAareGEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   369 TPKrevaskdmerrIVAQLLTCMDD----LNN-----VAATARVLVIGATNRPD----SLDPALRRagRF 425
Cdd:pfam07728  79 NPD-----------VLNSLLSLLDErrllLPDggelvKAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
617-719 7.16e-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: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   617 ILLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRR 689
Cdd:TIGR03922 315 MLFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
                          90       100       110
                  ....*....|....*....|....*....|
gi 32699478   690 SDRETGASVRVVNQLLTEMDGLETRQQVFI 719
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARMENDRDRLVVIG 421
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
617-687 7.66e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  617 ILLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 682
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                         90
                 ....*....|
gi 32699478  683 -----DALCP 687
Cdd:PRK13342 105 nkaqqDALLP 114
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
612-687 1.06e-06

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: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 612 GTPAGILLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFD 680
Cdd:COG2256  47 GRLSSMILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVD 112
                        90
                ....*....|....*
gi 32699478 681 EV--------DALCP 687
Cdd:COG2256 113 EIhrfnkaqqDALLP 127
PRK04195 PRK04195
replication factor C large subunit; Provisional
617-783 3.78e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.30  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  617 ILLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 688
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  689 RSDReTGAS--VRVVNqlltemdglETRQQVfILAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--VAILKTITKN- 763
Cdd:PRK04195 113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                        170       180
                 ....*....|....*....|....
gi 32699478  764 GTKppLDEDVnLETIAN----DLR 783
Cdd:PRK04195 177 GIE--CDDEA-LKEIAErsggDLR 197
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
298-356 4.14e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.35  E-value: 4.14e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32699478 298 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSgvsgeSEQKLRELFDQAVSNA 356
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYS-----AELKKTEFLMQALRKA 120
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
300-425 8.14e-06

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: 46.72  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDQAVSNAPC-IVFIDEIDAITPK-REVASK 377
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLAAILTNLEPGdVLFIDEIHRLNRAvEEILYP 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478   378 DMERRivaqlltCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 425
Cdd:pfam05496 107 AMEDF-------RLDIVIGKGPSARSIrldlppftLVGATTRAGLLTSPLR--DRF 153
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
300-373 1.16e-05

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.59  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV-SGVSGES-EQKLRELFDQA---VSNAP-CIVFIDEIDAITPKRE 373
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLLQAAdydVERAQrGIVYIDEIDKIARKSE 132
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
589-779 1.28e-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: 47.85  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 589 RDELIMAILApvrnpdqfrTLGLGTPagILLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESE 659
Cdd:COG0714  17 QEELIELVLI---------ALLAGGH--LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 660 RAVRQ--VFQRaknsapcVIFFDEVDalcprRSDRETGASvrvvnqLLTEMD------GLETR---QQVFILAATNRPDI 728
Cdd:COG0714  86 FEFRPgpLFAN-------VLLADEIN-----RAPPKTQSA------LLEAMEerqvtiPGGTYklpEPFLVIATQNPIEQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478 729 ID-----PAILRpgRLDKTLFVGLPPPADRVAILKTiTKNGTKPPLDEDVNLETIA 779
Cdd:COG0714 148 EGtyplpEAQLD--RFLLKLYIGYPDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
298-429 1.39e-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: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   298 RGVLLHGPPGCGKTLLAHAIA------GELDLP-ILKVAAPEIVSGVSGESEQKLRELFDQAVSNapcIVFIDEIDAITP 370
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32699478   371 KREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPD-----SLDPALRRagRFDREV 429
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMENDRD-----RLVVIGAGYRKDldkflEVNEGLRS--RFTRVI 446
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
297-420 3.34e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.51  E-value: 3.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 297 PRGVLLHGPPGCGKTLLAHAIAGEL-------DLPILKVAAPEIVSGVSGEseqkLRELFDQAVSNApcIVfIDEIDAIT 369
Cdd:COG0470  18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGNHPD----LLELNPEEKSDQ--IG-IDQIRELG 90
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32699478 370 PKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPALR 420
Cdd:COG0470  91 EFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTIR 149
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
617-650 3.91e-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: 44.80  E-value: 3.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 32699478   617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 650
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
617-687 4.69e-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: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   617 ILLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 678
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 32699478   679 FDEVDALCP 687
Cdd:pfam07724  81 IDEIEKAHP 89
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
298-342 6.81e-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: 6.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 32699478   298 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSGVSGESE 342
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTE 97
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
300-425 7.84e-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: 45.75  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDqAVSN--APCIVFIDEIDAITPK-REVAS 376
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAA-ILTNleEGDVLFIDEIHRLSPAvEELLY 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 32699478   377 KDMERrivaqllTCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 425
Cdd:TIGR00635 103 PAMED-------FRLDIVIGKGPSARSVrldlppftLVGATTRAGMLTSPLR--DRF 150
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
617-650 8.00e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 8.00e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 32699478  617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 650
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
298-416 9.40e-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: 9.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 298 RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES--EQKLRELFDQAVSNAPCIVFIDEIDAI----TPK 371
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPK 106
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 32699478 372 REvasKDMERRIVAQLLTCMddLNNVAATARVLVIGATNRPDSLD 416
Cdd:cd19506 107 TE---KQLDPKRLKKDLPKI--LKSLKPEDRVLIVGTTSRPFEAD 146
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
616-669 1.05e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 1.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478   616 GILLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 669
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
300-370 1.19e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.12  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478  300 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELF---------DqavsnapcIVFIDEIDAITP 370
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKPGDLAailtnleegD--------VLFIDEIHRLSP 116
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
616-735 1.29e-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: 42.66  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   616 GILLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 683
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32699478   684 alcprRSDRETgasVRVVNQLLTE-----MDGLETRQ----QVFILAATNRPDI----IDPAILR 735
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
614-683 1.54e-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: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 614 PAGILLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIF 678
Cdd:cd19499  41 IGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVL 118

                ....*
gi 32699478 679 FDEVD 683
Cdd:cd19499 119 LDEIE 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
300-325 2.16e-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: 2.16e-04
                        10        20
                ....*....|....*....|....*.
gi 32699478 300 VLLHGPPGCGKTLLAHAIAGELDLPI 325
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
551-688 2.46e-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: 2.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 551 ELNDFIVAlaevQPSAKREGFVTVPNvTWADIGALEDIRDELimailapvrnpdqfrtlglgTPAGILLAGPPGCGKTLL 630
Cdd:cd19498   8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDEV--------------------TPKNILMIGPTGVGKTEI 62
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478 631 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 688
Cdd:cd19498  63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
616-663 2.51e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.51e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 32699478 616 GILLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 663
Cdd:COG1224  66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
617-726 2.54e-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: 42.51  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQVFQRAKNSAPCVIFFDEVDALCPR---RSD 691
Cdd:cd19506  29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKkvpKTE 108
                        90       100       110
                ....*....|....*....|....*....|....*
gi 32699478 692 RETGASvRVVNQLLTEMDGLETRQQVFILAATNRP 726
Cdd:cd19506 109 KQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
578-650 4.43e-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: 4.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32699478   578 TWADIGALEDIRDELIMAILAPVRNPDQfrtlglgtPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 650
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
300-360 4.81e-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: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   300 VLLHGPPGCGKTLLAHAIAGELdLPILKVAAPEIVSGVSGE--------------------SEQKLRELFDQAVSNAPCI 359
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSVYSRNPDDdfwdgytgqpvviiddfgqnPDGPDEAELIRLVSSTPYP 79

                  .
gi 32699478   360 V 360
Cdd:pfam00910  80 P 80
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
300-416 5.08e-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: 5.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 300 VLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVsgvsgeseqkLRELFDQAVSNAPCIVFIDEIDAITPKREVAS 376
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 32699478 377 KDMERRIVAQLLtcmddlnNVAATARVLVIgATNRPDSLD 416
Cdd:cd01120  71 SSELLEDLAKLL-------RAARNTGITVI-ATIHSDKFD 102
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
617-648 6.36e-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: 6.36e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLNFISVKGP 648
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
PRK08116 PRK08116
hypothetical protein; Validated
298-367 6.47e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.32  E-value: 6.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32699478  298 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVS---GVSGESEQKLRELFDQAVSNAPCIVfIDEIDA 367
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANELiekGVPVIFVNFPQLLNrikSTYKSSGKEDENEIIRSLVNADLLI-LDDLGA 189
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
589-720 7.91e-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: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   589 RDELIMAILapvrnpDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV---ANESGLNFISVKGPELLNMYVG----ESERA 661
Cdd:pfam13191   5 REEELEQLL------DALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 32699478   662 VRQVFQRAKNSAPcVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFIL 720
Cdd:pfam13191  79 LRQLLDELESSLL-EAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
301-369 1.01e-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: 41.00  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 301 LLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESE-----------------QKLRelfdQAVSNAPCIVfID 363
Cdd:cd19500  41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirghrrtyvgampgriiQALK----KAGTNNPVFL-LD 111

                ....*.
gi 32699478 364 EIDAIT 369
Cdd:cd19500 112 EIDKIG 117
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
300-370 1.42e-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: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478   300 VLLHGPPGCGKTLLAHAIAGELD-----LPI--------------LKVAAPEIVSgvSGESEQklreLFDQAVSNAPCIV 360
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgderaLIRidmseymeehsvsrLIGAPPGYVG--YEEGGQ----LTEAVRRKPYSIV 79
                          90
                  ....*....|
gi 32699478   361 FIDEIDAITP 370
Cdd:pfam07724  80 LIDEIEKAHP 89
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
617-685 1.95e-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: 1.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 685
Cdd:cd19500  40 LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
298-376 6.00e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 6.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32699478 298 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSG-VSGESEQKLRELFDQaVSNAPCIVfIDEIDAITPKRE 373
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNElKEARADGRLERLLKR-LAKVDLLI-LDELGYLPLDAE 177

                ...
gi 32699478 374 VAS 376
Cdd:COG1484 178 GAE 180
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
617-644 7.65e-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: 37.85  E-value: 7.65e-03
                        10        20
                ....*....|....*....|....*...
gi 32699478 617 ILLAGPPGCGKTLLAKAVANESGLNFIS 644
Cdd:cd02020   2 IAIDGPAGSGKSTVAKLLAKKLGLPYLD 29
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
617-644 8.81e-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: 38.17  E-value: 8.81e-03
                          10        20
                  ....*....|....*....|....*...
gi 32699478   617 ILLAGPPGCGKTLLAKAVANESGLNFIS 644
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLIS 30
PRK13764 PRK13764
ATPase; Provisional
616-636 9.78e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 39.44  E-value: 9.78e-03
                         10        20
                 ....*....|....*....|.
gi 32699478  616 GILLAGPPGCGKTLLAKAVAN 636
Cdd:PRK13764 259 GILIAGAPGAGKSTFAQALAE 279
PRK04182 PRK04182
cytidylate kinase; Provisional
617-644 9.84e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 37.86  E-value: 9.84e-03
                         10        20
                 ....*....|....*....|....*...
gi 32699478  617 ILLAGPPGCGKTLLAKAVANESGLNFIS 644
Cdd:PRK04182   3 ITISGPPGSGKTTVARLLAEKLGLKHVS 30
 
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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