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Conserved domains on  [gi|755495862|ref|XP_011237158|]
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nuclear valosin-containing protein-like isoform X1 [Mus musculus]

Protein Classification

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 ...
220-833 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: 572.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  220 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 298
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  299 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 378
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  379 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 458
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  459 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 538
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  539 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 618
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  619 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 697
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  698 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 777
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862  778 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 833
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
Nucleolin_bd super family cl25070
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
24-50 2.72e-09

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


The actual alignment was detected with superfamily member pfam16725:

Pssm-ID: 465247  Cd Length: 70  Bit Score: 54.17  E-value: 2.72e-09
                          10        20
                  ....*....|....*....|....*..
gi 755495862   24 DYGRRKRNAFRIQVEKVFSIISSEKEL 50
Cdd:pfam16725  44 EYGRRKRNAFRIQVEKAYEIISREYGL 70
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
220-833 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: 572.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  220 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 298
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  299 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 378
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  379 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 458
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  459 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 538
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  539 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 618
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  619 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 697
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  698 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 777
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862  778 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 833
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 ...
243-409 3.31e-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: 3.31e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 321
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 322 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 400
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 755495862 401 GRFDREVCL 409
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
484-817 2.14e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 330.04  E-value: 2.14e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 484 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 563
Cdd:COG1222    8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 564 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 643
Cdd:COG1222   84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 644 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
Cdd:COG1222  164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 723 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 802
Cdd:COG1222  244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                        330
                 ....*....|....*
gi 755495862 803 KHFEDAFKKVKPSIS 817
Cdd:COG1222  308 EDLEKAIEKVKKKTE 322
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
530-824 1.18e-77

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 1.18e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 530 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 603
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 604 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 680
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 681 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 759
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 760 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 824
Cdd:PRK03992 333 T--EGASGADLKAICTEAGMFAIRDDRTE-----------VTMEDFLKAIEKVmgkeEKDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
595-725 2.24e-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: 189.34  E-value: 2.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 674
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755495862  675 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 725
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
553-826 4.67e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 180.70  E-value: 4.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 704
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 705 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 784
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755495862 785 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 826
Cdd:NF041006 327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
cell_div_CdvC NF041006
cell division protein CdvC;
238-463 1.23e-36

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.18  E-value: 1.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 238 NVKFEDVGG-NDAtlKEVCKMLI--HMRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSG 314
Cdd:NF041006  99 KVTFSDIVGlEDV--KEALKEAIvyPSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 315 VSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGAT 387
Cdd:NF041006 174 WLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGAT 250
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862 388 NRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 463
Cdd:NF041006 251 NKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
591-726 8.02e-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: 83.96  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862   591 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 653
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862   654 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 726
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
24-50 2.72e-09

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: 54.17  E-value: 2.72e-09
                          10        20
                  ....*....|....*....|....*..
gi 755495862   24 DYGRRKRNAFRIQVEKVFSIISSEKEL 50
Cdd:pfam16725  44 EYGRRKRNAFRIQVEKAYEIISREYGL 70
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
220-833 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: 572.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  220 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 298
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  299 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 378
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  379 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 458
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  459 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 538
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  539 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 618
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  619 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 697
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  698 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 777
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862  778 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 833
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 ...
243-409 3.31e-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: 3.31e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 321
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 322 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 400
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 755495862 401 GRFDREVCL 409
Cdd:cd19518  161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
484-817 2.14e-106

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 330.04  E-value: 2.14e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 484 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 563
Cdd:COG1222    8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 564 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 643
Cdd:COG1222   84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 644 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
Cdd:COG1222  164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 723 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 802
Cdd:COG1222  244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                        330
                 ....*....|....*
gi 755495862 803 KHFEDAFKKVKPSIS 817
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 ...
563-723 1.40e-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: 311.34  E-value: 1.40e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 563 LEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 642
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 643 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 755495862 723 V 723
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 ...
566-723 9.63e-92

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 285.33  E-value: 9.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 566 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 645
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 646 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 723
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
231-463 5.26e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 281.89  E-value: 5.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 231 STELQISNVKFEDVGGNDATLKEVCKMLI-HMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP 309
Cdd:COG1222   67 AVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 310 EIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATN 388
Cdd:COG1222  147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATN 223
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755495862 389 RPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 463
Cdd:COG1222  224 RPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
465-813 1.09e-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: 1.09e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 465 RVLMKQQAQQKKKPEIEGLPSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSA 544
Cdd:COG0464   64 ALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 545 KREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVK 624
Cdd:COG0464  144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 625 GPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLetRQQVFILAATNRP 704
Cdd:COG0464  224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRP 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 705 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 784
Cdd:COG0464  302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL 374
                        330       340
                 ....*....|....*....|....*....
gi 755495862 785 eitaqkngvgaGELKVSHKHFEDAFKKVK 813
Cdd:COG0464  375 -----------GREPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
530-824 1.18e-77

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 1.18e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 530 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 603
Cdd:PRK03992  98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 604 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 680
Cdd:PRK03992 177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 681 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 759
Cdd:PRK03992 256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 760 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 824
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 ...
243-409 3.53e-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: 244.51  E-value: 3.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 320
Cdd:cd19503    1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 321 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRA 400
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS---RGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 755495862 401 GRFDREVCL 409
Cdd:cd19503  157 GRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
241-463 6.97e-72

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 241.35  E-value: 6.97e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 241 FEDVGGNDATLKEVCKMLIHMRH-PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 319
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 320 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRR 399
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRS-----DVVVIAATNRPDLLDPALLR 310
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495862 400 agRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 463
Cdd:COG0464  311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
566-723 5.98e-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: 5.98e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 566 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 645
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 646 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 723
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 ...
566-723 3.03e-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: 225.85  E-value: 3.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 566 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 645
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 646 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 755495862 723 V 723
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 ...
559-719 5.39e-68

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 222.55  E-value: 5.39e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 638
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 639 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 718
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 .
gi 755495862 719 K 719
Cdd:cd19503  161 R 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
553-812 7.89e-67

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 230.64  E-value: 7.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  553 PNVTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  633 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRP 704
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  705 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 784
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVAR--RTPGFSGADLANLLNEAALLAARK 278
                         250       260
                  ....*....|....*....|....*...
gi 755495862  785 EITAqkngvgagelkVSHKHFEDAFKKV 812
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 ...
566-722 1.67e-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: 218.07  E-value: 1.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 566 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 645
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862 646 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
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 ...
243-410 2.19e-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: 218.07  E-value: 2.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 321
Cdd:cd19519    1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 322 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAG 401
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK---QRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 755495862 402 RFDREVCLG 410
Cdd:cd19519  158 RFDREIDIG 166
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
225-463 3.05e-64

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 220.47  E-value: 3.05e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 225 KKAKARSTELQIS-NVKFEDVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDL 301
Cdd:PRK03992 113 KDPRVQAMEVIESpNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNA 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 302 PILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaT 378
Cdd:PRK03992 192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---R 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 379 ARVLVIGATNRPDSLDPALRRAGRFDR--EVCLgiPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCR 456
Cdd:PRK03992 269 GNVKIIAATNRIDILDPAILRPGRFDRiiEVPL--PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICT 346

                 ....*..
gi 755495862 457 EAAMCAV 463
Cdd:PRK03992 347 EAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
226-465 1.15e-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: 222.16  E-value: 1.15e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  226 KAKARSTELQISNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 305
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  306 VAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKRE---VASKDMERRIVAQLLTCMDDLNNvaaTARVL 382
Cdd:TIGR01241 119 ISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT---NTGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  383 VIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCA 462
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275

                  ...
gi 755495862  463 VNR 465
Cdd:TIGR01241 276 ARK 278
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
562-723 3.60e-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: 206.36  E-value: 3.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 562 ALEDIRDelimaILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 641
Cdd:cd19481    1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 642 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKT 720
Cdd:cd19481   76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                 ...
gi 755495862 721 LFV 723
Cdd:cd19481  156 IEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
553-812 1.19e-61

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 218.75  E-value: 1.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADI-GA------LEDIRDELimailapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKG 625
Cdd:COG0465  137 PKVTFDDVaGVdeakeeLQEIVDFL--------KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 626 PELLNMYVG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLETRQQV 695
Cdd:COG0465  209 SDFVEMFVGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGV 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 696 FILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtKpPLDEDVNLETIANdlRCNCYTGADLTALVR 775
Cdd:COG0465  282 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIAR--RTPGFSGADLANLVN 356
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 755495862 776 EASLCALRqeitaqkngvgAGELKVSHKHFEDAFKKV 812
Cdd:COG0465  357 EAALLAAR-----------RNKKAVTMEDFEEAIDRV 382
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
566-723 6.29e-60

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 200.43  E-value: 6.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 566 IRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 645
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 646 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-TRQQVFILAATNRPDIIDPAILRPGRLDKTLF 722
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                 .
gi 755495862 723 V 723
Cdd:cd19527  160 L 160
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
226-465 6.48e-60

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 213.75  E-value: 6.48e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 226 KAKARSTELQISNVKFEDVGGND---ATLKEVCKMLihmRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLP 302
Cdd:COG0465  126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 303 ILKVAAPEIVS---GVsGESeqKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDmER-RIVAQLLTCMD--Dln 373
Cdd:COG0465  203 FFSISGSDFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGHD-EReQTLNQLLVEMDgfE-- 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 374 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 453
Cdd:COG0465  277 ---GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353
                        250
                 ....*....|..
gi 755495862 454 LCREAAMCAVNR 465
Cdd:COG0465  354 LVNEAALLAARR 365
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
556-719 9.10e-60

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 200.26  E-value: 9.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 556 TWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 635
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 636 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAIL 712
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*..
gi 755495862 713 RPGRLDK 719
Cdd:cd19502  161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
555-812 4.02e-59

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 212.99  E-value: 4.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 555 VTWADIGALEDIRDEL--IMAILapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFeeVVSFL---KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLETRQQVFILAATNRP 704
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRV 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 705 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 784
Cdd:CHL00176 332 DILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARR 406
                        250       260
                 ....*....|....*....|....*...
gi 755495862 785 EITaqkngvgagelKVSHKHFEDAFKKV 812
Cdd:CHL00176 407 KKA-----------TITMKEIDTAIDRV 423
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
555-723 1.18e-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: 197.45  E-value: 1.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 555 VTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 634
Cdd:cd19501    1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 635 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAI 711
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 755495862 712 LRPGRLDKTLFV 723
Cdd:cd19501  160 LRPGRFDRQVYV 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
241-458 2.40e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 196.64  E-value: 2.40e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 241 FEDVGGNDATlKEVCKMLIH-MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 319
Cdd:COG1223    1 LDDVVGQEEA-KKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 320 EQKLRELFDQAvSNAPCIVFIDEIDAITPKREVASKDME-RRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALR 398
Cdd:COG1223   80 ARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDGLPS-----GSVVIAATNHPELLDSALW 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 399 RagRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 458
Cdd:COG1223  154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
510-750 2.45e-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: 204.94  E-value: 2.45e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  510 GLLRDQDPLSEEQMQGLCIELndfiVALAEVQPSAKREgfvtVPNVTWADIGAL----EDIRDelimAILAPVRNPDQFR 585
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEA----IPRTEVEDLVLEE----VPDVTYADIGGLgsqiEQIRD----AVELPFLHPELYR 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  586 TLGLGTPAGILLAGPPGCGKTLLAKAVAN-------ESGLN---FISVKGPELLNMYVGESERAVRQVFQRAKNSA---- 651
Cdd:TIGR03689 210 EYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegr 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  652 PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLP 726
Cdd:TIGR03689 290 PVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERP 365
                         250       260
                  ....*....|....*....|....*
gi 755495862  727 PPADRVAIL-KTITKNgtkPPLDED 750
Cdd:TIGR03689 366 DAEAAADIFaKYLTDD---LPLPED 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
595-725 2.24e-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: 189.34  E-value: 2.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 674
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755495862  675 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 725
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 ...
559-724 6.84e-56

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 189.57  E-value: 6.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 638
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 639 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 718
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 755495862 719 KTLFVG 724
Cdd:cd19519  161 REIDIG 166
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
553-812 7.39e-56

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 197.68  E-value: 7.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 709
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 710 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRqeitaq 789
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAICQEAGMQAVR------ 368
                        250       260
                 ....*....|....*....|...
gi 755495862 790 KNgvgagELKVSHKHFEDAFKKV 812
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 ...
260-407 6.00e-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: 186.72  E-value: 6.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 260 HMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVF 339
Cdd:cd19481   12 PRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILF 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 340 IDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREV 407
Cdd:cd19481   91 IDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
251-405 3.89e-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: 184.41  E-value: 3.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 251 LKEVCKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFD 328
Cdd:cd19511    1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755495862 329 QAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDR 405
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
556-830 5.81e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 198.33  E-value: 5.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 556 TWADIGALEDIRDElIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 635
Cdd:PRK10733 150 TFADVAGCDEAKEE-VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 636 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLETRQQVFILAATNRPDII 707
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 708 DPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDlrCNCYTGADLTALVREASLCALRqeit 787
Cdd:PRK10733 304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 755495862 788 aqkngvgAGELKVSHKHFEDAFKKVKPSISIKDQVMYEALQRS 830
Cdd:PRK10733 375 -------GNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
226-462 3.84e-53

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 196.02  E-value: 3.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 226 KAKARS-TELQISNVkFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPIL 304
Cdd:PRK10733 136 KSKARMlTEDQIKTT-FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 305 KVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREV---ASKDMERRIVAQLLTCMDDLNnvaATARV 381
Cdd:PRK10733 215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE---GNEGI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 382 LVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMC 461
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371

                 .
gi 755495862 462 A 462
Cdd:PRK10733 372 A 372
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
278-410 2.39e-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: 178.56  E-value: 2.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDM 357
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755495862  358 ERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREVCLG 410
Cdd:pfam00004  81 SRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
239-407 5.35e-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: 178.97  E-value: 5.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 239 VKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 318
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 319 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDMERRIVAQLLTCMDDLnnvAATARVLVIGATNRPDSLDP 395
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGF---ESNTGVIVIAATNRPDVLDP 157
                        170
                 ....*....|..
gi 755495862 396 ALRRAGRFDREV 407
Cdd:cd19501  158 ALLRPGRFDRQV 169
ftsH CHL00176
cell division protein; Validated
217-465 7.38e-52

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.19  E-value: 7.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 217 GEIEALLQKKAKarstelqiSNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIA 296
Cdd:CHL00176 166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 297 GELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDMER-RIVAQLLTCMDDLN 373
Cdd:CHL00176 238 GEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEReQTLNQLLTEMDGFK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 374 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 453
Cdd:CHL00176 318 ---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLAN 394
                        250
                 ....*....|..
gi 755495862 454 LCREAAMCAVNR 465
Cdd:CHL00176 395 LLNEAAILTARR 406
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
574-813 1.38e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.77  E-value: 1.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 574 ILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNsAPC 653
Cdd:COG1223   17 IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFARR-APC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 654 VIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLetRQQVFILAATNRPDIIDPAILRpgRLDKTLFVGLPPPADRV 732
Cdd:COG1223   96 VIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 733 AILKtitKNGTKPPLDEDVNLETIANdlRCNCYTGADLTALVREaslcALRQEITAQKNgvgagelKVSHKHFEDAFKKV 812
Cdd:COG1223  172 EILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----ALKKAILEDRE-------KVTKEDLEEALKQR 235

                 .
gi 755495862 813 K 813
Cdd:COG1223  236 K 236
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
559-719 1.75e-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: 1.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 638
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 639 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----ETRQQVFILAATNRPDIIDPAILRP 714
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*
gi 755495862 715 GRLDK 719
Cdd:cd19518  161 GRFDR 165
cell_div_CdvC NF041006
cell division protein CdvC;
553-826 4.67e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 180.70  E-value: 4.67e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 704
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 705 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 784
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 755495862 785 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 826
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 ...
560-723 7.06e-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: 172.92  E-value: 7.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 560 IGALEDIRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 639
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 640 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpgRL 717
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 755495862 718 DKTLFV 723
Cdd:cd19509  158 EKRIYI 163
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
241-407 2.18e-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: 171.75  E-value: 2.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 241 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 319
Cdd:cd19502    2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 320 EQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPA 396
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFD---PRGNIKVIMATNRPDILDPA 158
                        170
                 ....*....|.
gi 755495862 397 LRRAGRFDREV 407
Cdd:cd19502  159 LLRPGRFDRKI 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
238-465 3.35e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 178.80  E-value: 3.35e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 238 NVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVS 316
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 317 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMER---RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSL 393
Cdd:PTZ00454 221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQ---TTNVKVIMATNRADTL 297
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755495862 394 DPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAVNR 465
Cdd:PTZ00454 298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
261-407 5.68e-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: 5.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 261 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 340
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755495862 341 DEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREV 407
Cdd:cd19529   93 DEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDIIDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
241-463 1.08e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 173.03  E-value: 1.08e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 241 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 319
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 320 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 399
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495862 400 AGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 463
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
553-812 3.45e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.49  E-value: 3.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 709
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 710 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIAN---DLrcncyTGADLTALVREASLCALRQEi 786
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFIMakdEL-----SGADIKAICTEAGLLALRER- 408
                        250       260
                 ....*....|....*....|....*.
gi 755495862 787 taqkngvgagELKVSHKHFEDAFKKV 812
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 ...
263-405 2.17e-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: 159.98  E-value: 2.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 263 HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDE 342
Cdd:cd19528   15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDE 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862 343 IDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 405
Cdd:cd19528   95 LDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
243-406 2.22e-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: 157.67  E-value: 2.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVCKM-LIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA-----APEIVSGVS 316
Cdd:cd19517    1 DIGGLSHYINQLKEMvFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 317 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPA 396
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|
gi 755495862 397 LRRAGRFDRE 406
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 ...
261-405 4.22e-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: 153.80  E-value: 4.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 261 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 340
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755495862 341 DEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 405
Cdd:cd19530   96 DEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
559-722 6.06e-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: 153.43  E-value: 6.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 633
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 634 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILR 713
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*....
gi 755495862 714 PGRLDKTLF 722
Cdd:cd19517  161 PGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
553-723 6.21e-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: 6.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 631
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 632 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-ETRQQVFILAATNRPDIIDPA 710
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 755495862 711 ILRpgRLDKTLFV 723
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
559-723 6.82e-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: 150.65  E-value: 6.82e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLGL-GTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 637
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 638 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpg 715
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAILR-- 158

                 ....*...
gi 755495862 716 RLDKTLFV 723
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 ...
262-407 2.22e-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: 148.73  E-value: 2.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 262 RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFID 341
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862 342 EIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 407
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 ...
244-407 5.28e-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: 5.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 244 VGGND---ATLKEVckMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 320
Cdd:cd19509    1 IAGLDdakEALKEA--VILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 321 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRa 400
Cdd:cd19509   78 KIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN-KPEDRVLVLGATNRPWELDEAFLR- 155

                 ....*..
gi 755495862 401 gRFDREV 407
Cdd:cd19509  156 -RFEKRI 161
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
559-723 1.07e-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: 1.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 637
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 638 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------ETRQQVFILAATNRPDIIDP 709
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 755495862 710 AILRpgRLDKTLFV 723
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 ...
261-405 1.25e-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: 138.03  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 261 MRHPEVYQhLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 340
Cdd:cd19527   13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862 341 DEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRRAGRFDR 405
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; ...
553-723 7.74e-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: 137.04  E-value: 7.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 553 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 632
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 633 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPA 710
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 755495862 711 ILRpgRLDKTLFV 723
Cdd:cd19525  176 ARR--RLVKRLYI 186
cell_div_CdvC NF041006
cell division protein CdvC;
238-463 1.23e-36

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.18  E-value: 1.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 238 NVKFEDVGG-NDAtlKEVCKMLI--HMRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSG 314
Cdd:NF041006  99 KVTFSDIVGlEDV--KEALKEAIvyPSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSK 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 315 VSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGAT 387
Cdd:NF041006 174 WLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGAT 250
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862 388 NRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 463
Cdd:NF041006 251 NKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
560-718 1.83e-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: 132.61  E-value: 1.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 560 IGALE-DIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYV 633
Cdd:cd19504    2 IGGLDkEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 634 GESERAVRQVF------QRAK--NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLETRQQVFILAATNR 703
Cdd:cd19504   78 GESEANIRKLFadaeeeQRRLgaNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNR 157
                        170
                 ....*....|....*
gi 755495862 704 PDIIDPAILRPGRLD 718
Cdd:cd19504  158 KDLIDEALLRPGRLE 172
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
238-421 1.97e-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: 1.97e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  238 NVKFEDVGGNDATLKevckmLIH------MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPI-------- 303
Cdd:TIGR03689 178 DVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIgaegggks 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  304 --LKVAAPEIVSGVSGESEQKLRELFDQAVSNA----PCIVFIDEIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVA 376
Cdd:TIGR03689 253 yfLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 755495862  377 ATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERIL 421
Cdd:TIGR03689 330 SLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
559-723 2.29e-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: 128.81  E-value: 2.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTPA-GILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 637
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 638 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpg 715
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 755495862 716 RLDKTLFV 723
Cdd:cd19524  157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
238-407 4.59e-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: 4.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 238 NVKFEDVGGNDATlKEVCK--MLIHMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 315
Cdd:cd19521    3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 316 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDP 395
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGN--DSQGVLVLGATNIPWQLDS 158
                        170
                 ....*....|..
gi 755495862 396 ALRRagRFDREV 407
Cdd:cd19521  159 AIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
243-399 7.26e-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: 7.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGND---ATLKEvcKMLIHMRHPEVYQHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 318
Cdd:cd19520    1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 319 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALR 398
Cdd:cd19520   79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLST-DGNCRVIVMGATNRPQDLDEAIL 157

                 .
gi 755495862 399 R 399
Cdd:cd19520  158 R 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
239-399 6.53e-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: 6.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 239 VKFEDVGGND---ATLKEVckMLIHMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 315
Cdd:cd19525   19 INWADIAGLEfakKTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 316 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLnNVAATARVLVIGATNRPDSLDP 395
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGA-TTSSEDRILVVGATNRPQEIDE 174

                 ....
gi 755495862 396 ALRR 399
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 ...
559-723 1.10e-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: 1.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELimailaPVRNP---DQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 635
Cdd:cd19507    1 DVGGLDNLKDWL------KKRKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 636 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAATNRPDIIDPAILRP 714
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*....
gi 755495862 715 GRLDKTLFV 723
Cdd:cd19507  153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
589-725 8.61e-29

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 112.62  E-value: 8.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 589 LGTPAGILLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFDEVDA 662
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862 663 LCPRrsdretgASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGL 725
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 ...
271-405 4.84e-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: 4.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 271 GVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPK 349
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862 350 REVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDR 405
Cdd:cd19507  107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
249-399 3.07e-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: 3.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 249 ATLKEVCKML-----IHMRHPEVYQhlGVVPP-RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQK 322
Cdd:cd19522    3 ADLEEAKKLLeeavvLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 323 LRELFDQAVSNAPCIVFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPAL 397
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEAL 160

                 ..
gi 755495862 398 RR 399
Cdd:cd19522  161 RR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
243-399 9.27e-27

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: 107.24  E-value: 9.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGNDATLKEVCKMLI-HMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 321
Cdd:cd19524    1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 322 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPA-LRR 399
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS-NGDDRVLVMGATNRPQELDDAvLRR 157
ycf46 CHL00195
Ycf46; Provisional
237-451 9.95e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 114.73  E-value: 9.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 237 SNVKFEDVGGNDatlkeVCKMLIHMRH---PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVS 313
Cdd:CHL00195 223 VNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 314 GVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDS 392
Cdd:CHL00195 298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755495862 393 LDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRlP---ETFNFCHLAHLTPGFVGADL 451
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIKKLSKLSNKFSGAEI 433
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
274-410 9.99e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 106.46  E-value: 9.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 274 PPRGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSGVSGESEQK---LRELFDQAVSNAPCIVFIDEIDAIT 347
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDSLS 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495862 348 pkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGRFDREVCLG 410
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; ...
244-407 1.16e-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: 104.49  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 244 VGGNDATLKEVCKMLIHMR--HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK-VAAPEIVSGVSGESE 320
Cdd:cd19504    2 IGGLDKEFSDIFRRAFASRvfPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 321 QKLRELFDQA---------VSNAPCIVFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNvaatarVLVIGA 386
Cdd:cd19504   82 ANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNN------ILVIGM 154
                        170       180
                 ....*....|....*....|.
gi 755495862 387 TNRPDSLDPALRRAGRFDREV 407
Cdd:cd19504  155 TNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
498-777 1.02e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 108.57  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 498 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVALAEVQPSA-------KRE--------GFV 550
Cdd:CHL00195 144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATYKTIDENSiplileeKKQiisqteilEFY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 551 TVpNVTWADIGALEDIRDELimailapvrnpdQFRT---------LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFI 621
Cdd:CHL00195 222 SV-NEKISDIGGLDNLKDWL------------KKRStsfskqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 622 SVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAA 700
Cdd:CHL00195 289 RLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVAT 366
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862 701 TNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKtITKNGTKPPLDEDVNLETIAndLRCNCYTGADLTALVREA 777
Cdd:CHL00195 367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFK-IHLQKFRPKSWKKYDIKKLS--KLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
559-723 2.02e-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: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 559 DIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 638
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 639 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpgR 716
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGsgEDGVLVVCTTSKPEEIDESLRR--Y 156

                 ....*..
gi 755495862 717 LDKTLFV 723
Cdd:cd19523  157 FSKRLLV 163
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
243-399 1.18e-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: 86.86  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 243 DVGGND---ATLKEvcKMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 319
Cdd:cd19523    1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 320 EQKLRELFDQAVSNAPCIVFIDEIDAITPKReVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRR 399
Cdd:cd19523   78 EKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLG-SGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
591-726 8.02e-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: 83.96  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862   591 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 653
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862   654 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 726
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
274-413 8.67e-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: 83.96  E-value: 8.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862   274 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFDQAVSNAPC 336
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862   337 IVFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREVCLGIPD 413
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
261-407 3.28e-18

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 82.40  E-value: 3.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 261 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESEQKLRELfdqavSNAP--CIV 338
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLL-----NTAPkqSII 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755495862 339 FIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 407
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 ...
595-710 3.31e-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: 69.01  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 659
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755495862 660 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPA 710
Cdd:cd19508  134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
578-718 3.69e-12

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 65.07  E-value: 3.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 578 VRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 656
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755495862 657 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 718
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 ...
595-711 1.06e-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: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 673
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755495862 674 ASVR-VVNQLLTEMdGLETRQQVFILaATNRPDIIDPAI 711
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 ...
276-407 1.14e-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: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIA--GELDLPILKVA--APEIVSGVSgeseqKLRELFDQA-VSNAPCIVFIDEIDAITPKR 350
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGdvAPMGREGVT-----AIHKVFDWAnTSRRGLLLFVDEADAFLRKR 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 351 --EVASKDMeRRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRraGRFDREV 407
Cdd:cd19512   98 stEKISEDL-RAALNAFLYRTGEQSN-----KFMLVLASNQPEQFDWAIN--DRIDEMV 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
278-343 1.62e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.95  E-value: 1.62e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVsgeseQKLRELFDQAVSNA----PCIVFIDEI 343
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; ...
587-719 1.99e-10

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 60.08  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 587 LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 652
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755495862 653 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLETRQQVFIlAATNRPDIIDPAILRPGRLDK 719
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
278-343 2.06e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.92  E-value: 2.06e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVSgeseqKLRELFDQA----VSNAPCIVFIDEI 343
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 ...
276-397 7.64e-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: 7.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIAGELDL---------PILKVAAPEIVSGVSGESEQKLRELFDQA---VSNAPCIVF--ID 341
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKDALVFvlID 132
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 342 EIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 397
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; ...
269-405 1.35e-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: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 269 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA--------------APEIVSGVSGESEQKLRELFDQAVSNA 334
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755495862 335 PCIVFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDR 405
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
Nucleolin_bd pfam16725
Nucleolin binding domain; This domain adopts a three helix fold resembling part of a winged ...
24-50 2.72e-09

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: 54.17  E-value: 2.72e-09
                          10        20
                  ....*....|....*....|....*..
gi 755495862   24 DYGRRKRNAFRIQVEKVFSIISSEKEL 50
Cdd:pfam16725  44 EYGRRKRNAFRIQVEKAYEIISREYGL 70
PRK04195 PRK04195
replication factor C large subunit; Provisional
240-349 5.04e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.55  E-value: 5.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 240 KFEDVGGNDATLKEVCKMLihmrhpEVYQHlgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP-----EIVSG 314
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI------ESWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIER 83
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755495862 315 VSGESEQKlRELFDQAVSnapcIVFIDEIDAITPK 349
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 ...
434-467 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 755495862  434 FNFCHLAHLTPGFVGADLMALCREAAMCAVNRVL 467
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 ...
750-807 4.37e-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: 4.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 755495862  750 DVNLETIANdlRCNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFED 807
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 ...
273-403 6.41e-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: 53.54  E-value: 6.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 273 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEI--VSGVSGESEQKLRELFDQavsnapcIVFIDEIDAITPKR 350
Cdd:cd19498   44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVEG-------IVFIDEIDKIAKRG 116
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862 351 EVASKDMERRIVAQLL------TCMDDLNNVAATARVLVIGA----TNRPDSLDPALRraGRF 403
Cdd:cd19498  117 GSSGPDVSREGVQRDLlpivegSTVSTKYGPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
278-459 1.06e-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: 54.40  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAA-----PEIVSGVS------GESEQKLRELFDQavsnapcIVFIDEIDAI 346
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllPSDILGTYiydqqtGEFEFRPGPLFAN-------VLLADEINRA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 347 TPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS-----LDPALRRagRFDREVCLGIPDEA 415
Cdd:COG0714  107 PPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPDAE 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755495862 416 ARERILqtlcrKLRLPEtfnfcHLAHLTPGFVGADLMALCREAA 459
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 ...
277-403 3.16e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 50.37  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  277 GVLLHGPPGCGKTLLAHAIAGELD-LPILKVAAP------EIVSGVsgESEQKLRELFDQAVSNA---PCIVFIDEIDAI 346
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRR--NIDPGGASWVDGPLVRAareGEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  347 TPKrevaskdmerrIVAQLLTCMDD----LNN-----VAATARVLVIGATNRPD----SLDPALRRagRF 403
Cdd:pfam07728  79 NPD-----------VLNSLLSLLDErrllLPDggelvKAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
595-665 6.61e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 6.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 660
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                         90
                 ....*....|
gi 755495862 661 -----DALCP 665
Cdd:PRK13342 105 nkaqqDALLP 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
595-697 6.92e-07

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 52.92  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  595 ILLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRR 667
Cdd:TIGR03922 315 MLFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
                          90       100       110
                  ....*....|....*....|....*....|
gi 755495862  668 SDRETGASVRVVNQLLTEMDGLETRQQVFI 697
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARMENDRDRLVVIG 421
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
590-665 9.11e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 52.37  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 590 GTPAGILLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFD 658
Cdd:COG2256   47 GRLSSMILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVD 112
                         90
                 ....*....|....*
gi 755495862 659 EV--------DALCP 665
Cdd:COG2256  113 EIhrfnkaqqDALLP 127
PRK04195 PRK04195
replication factor C large subunit; Provisional
595-761 3.32e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.30  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 666
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 667 RSDReTGAS--VRVVNqlltemdglETRQQVfILAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--VAILKTITKN- 741
Cdd:PRK04195 113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                        170       180
                 ....*....|....*....|....
gi 755495862 742 GTKppLDEDVnLETIAN----DLR 761
Cdd:PRK04195 177 GIE--CDDEA-LKEIAErsggDLR 197
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
276-334 3.87e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.35  E-value: 3.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSgvsgeSEQKLRELFDQAVSNA 334
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 ...
278-403 7.12e-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: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDQAVSNAPC-IVFIDEIDAITPK-REVASK 355
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLAAILTNLEPGdVLFIDEIHRLNRAvEEILYP 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862  356 DMERRivaqlltCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 403
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 ...
278-351 1.04e-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: 47.98  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV-SGVSGES-E---QKLRELFDQAVSNAP-CIVFIDEIDAITPKRE 351
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvEnilLKLLQAADYDVERAQrGIVYIDEIDKIARKSE 132
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
567-757 1.04e-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: 48.24  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 567 RDELIMAILApvrnpdqfrTLGLGTPagILLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESE 637
Cdd:COG0714   17 QEELIELVLI---------ALLAGGH--LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 638 RAVRQ--VFQRaknsapcVIFFDEVDalcprRSDRETGASvrvvnqLLTEMD------GLETR---QQVFILAATNRPDI 706
Cdd:COG0714   86 FEFRPgpLFAN-------VLLADEIN-----RAPPKTQSA------LLEAMEerqvtiPGGTYklpEPFLVIATQNPIEQ 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862 707 ID-----PAILRpgRLDKTLFVGLPPPADRVAILKTiTKNGTKPPLDEDVNLETIA 757
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 ...
276-407 1.32e-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: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  276 RGVLLHGPPGCGKTLLAHAIA------GELDLP-ILKVAAPEIVSGVSGESEQKLRELFDQAVSNapcIVFIDEIDAITP 348
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755495862  349 KREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPD-----SLDPALRRagRFDREV 407
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMENDRD-----RLVVIGAGYRKDldkflEVNEGLRS--RFTRVI 446
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
595-628 3.48e-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: 3.48e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755495862  595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 628
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
275-398 3.66e-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: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 275 PRGVLLHGPPGCGKTLLAHAIAGEL-------DLPILKVAAPEIVSGVSGEseqkLRELFDQAVSNApcIVfIDEIDAIT 347
Cdd:COG0470   18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGNHPD----LLELNPEEKSDQ--IG-IDQIRELG 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755495862 348 PKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPALR 398
Cdd:COG0470   91 EFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTIR 149
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
595-665 4.22e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.88  E-value: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  595 ILLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 656
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 755495862  657 FDEVDALCP 665
Cdd:pfam07724  81 IDEIEKAHP 89
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
276-320 6.48e-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: 6.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755495862  276 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSGVSGESE 320
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTE 97
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
278-403 7.20e-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: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDqAVSN--APCIVFIDEIDAITPK-REVAS 354
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAA-ILTNleEGDVLFIDEIHRLSPAvEELLY 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755495862  355 KDMERrivaqllTCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 403
Cdd:TIGR00635 103 PAMED-------FRLDIVIGKGPSARSVrldlppftLVGATTRAGMLTSPLR--DRF 150
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
595-628 7.55e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 7.55e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 628
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 ...
276-394 7.77e-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: 44.06  E-value: 7.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES--EQKLRELFDQAVSNAPCIVFIDEIDAI----TPK 349
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPK 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755495862 350 REvasKDMERRIVAQLLTCMddLNNVAATARVLVIGATNRPDSLD 394
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 ...
594-647 9.87e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 9.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862  594 GILLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 647
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
278-348 1.05e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.12  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELF---------DqavsnapcIVFIDEIDAITP 348
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 ...
594-713 1.08e-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: 43.05  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  594 GILLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 661
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755495862  662 alcprRSDRETgasVRVVNQLLTE-----MDGLETRQ----QVFILAATNRPDI----IDPAILR 713
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
592-661 1.34e-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: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 592 PAGILLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIF 656
Cdd:cd19499   41 IGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVL 118

                 ....*
gi 755495862 657 FDEVD 661
Cdd:cd19499  119 LDEIE 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
278-303 1.94e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 44.30  E-value: 1.94e-04
                         10        20
                 ....*....|....*....|....*.
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGELDLPI 303
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
595-704 2.16e-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: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQVFQRAKNSAPCVIFFDEVDALCPR---RSD 669
Cdd:cd19506   29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKkvpKTE 108
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 755495862 670 RETGASvRVVNQLLTEMDGLETRQQVFILAATNRP 704
Cdd:cd19506  109 KQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
529-666 2.24e-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: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 529 ELNDFIVAlaevQPSAKREGFVTVPNvTWADIGALEDIRDELimailapvrnpdqfrtlglgTPAGILLAGPPGCGKTLL 608
Cdd:cd19498    8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDEV--------------------TPKNILMIGPTGVGKTEI 62
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862 609 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 666
Cdd:cd19498   63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
594-641 2.33e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755495862 594 GILLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 641
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
556-628 4.15e-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: 43.44  E-value: 4.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755495862  556 TWADIGALEDIRDELIMAILAPVRNPDQfrtlglgtPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 628
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
278-394 4.53e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 40.56  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 278 VLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVsgvsgeseqkLRELFDQAVSNAPCIVFIDEIDAITPKREVAS 354
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755495862 355 KDMERRIVAQLLtcmddlnNVAATARVLVIgATNRPDSLD 394
Cdd:cd01120   71 SSELLEDLAKLL-------RAARNTGITVI-ATIHSDKFD 102
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
278-338 4.67e-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: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  278 VLLHGPPGCGKTLLAHAIAGELdLPILKVAAPEIVSGVSGE--------------------SEQKLRELFDQAVSNAPCI 337
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSVYSRNPDDdfwdgytgqpvviiddfgqnPDGPDEAELIRLVSSTPYP 79

                  .
gi 755495862  338 V 338
Cdd:pfam00910  80 P 80
PRK08116 PRK08116
hypothetical protein; Validated
276-345 5.73e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.70  E-value: 5.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVS---GVSGESEQKLRELFDQAVSNAPCIVfIDEIDA 345
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANELiekGVPVIFVNFPQLLNrikSTYKSSGKEDENEIIRSLVNADLLI-LDDLGA 189
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
595-626 5.74e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.76  E-value: 5.74e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFISVKGP 626
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
567-698 6.93e-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: 41.34  E-value: 6.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  567 RDELIMAILapvrnpDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV---ANESGLNFISVKGPELLNMYVG----ESERA 639
Cdd:pfam13191   5 REEELEQLL------DALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755495862  640 VRQVFQRAKNSAPcVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFIL 698
Cdd:pfam13191  79 LRQLLDELESSLL-EAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
279-347 8.67e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.00  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 279 LLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESE-----------------QKLRelfdQAVSNAPCIVfID 341
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirghrrtyvgampgriiQALK----KAGTNNPVFL-LD 111

                 ....*.
gi 755495862 342 EIDAIT 347
Cdd:cd19500  112 EIDKIG 117
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
278-348 1.24e-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: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862  278 VLLHGPPGCGKTLLAHAIAGELD-----LPI--------------LKVAAPEIVSgvSGESEQklreLFDQAVSNAPCIV 338
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgderaLIRidmseymeehsvsrLIGAPPGYVG--YEEGGQ----LTEAVRRKPYSIV 79
                          90
                  ....*....|
gi 755495862  339 FIDEIDAITP 348
Cdd:pfam07724  80 LIDEIEKAHP 89
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
595-663 1.76e-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: 1.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 663
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
276-354 5.42e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 276 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSG-VSGESEQKLRELFDQaVSNAPCIVfIDEIDAITPKRE 351
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNElKEARADGRLERLLKR-LAKVDLLI-LDELGYLPLDAE 177

                 ...
gi 755495862 352 VAS 354
Cdd:COG1484  178 GAE 180
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
595-622 6.96e-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: 6.96e-03
                         10        20
                 ....*....|....*....|....*...
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFIS 622
Cdd:cd02020    2 IAIDGPAGSGKSTVAKLLAKKLGLPYLD 29
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
275-429 7.77e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 275 PRG--VLLHGPPGCGKTLLAHAIAGELdlpilkVAAPE---IVSgvSGESEQKLREL-------FDQAVSNApCIVFIDe 342
Cdd:COG0467   18 PRGssTLLSGPPGTGKTTLALQFLAEG------LRRGEkglYVS--FEESPEQLLRRaeslgldLEEYIESG-LLRIID- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755495862 343 idaITPKREVASKDMerrIVAQLLTCMDDLNnvaatARVLVIgatnrpDSLDpALRRAgrfdrevclgIPDEAARERILQ 422
Cdd:COG0467   88 ---LSPEELGLDLEE---LLARLREAVEEFG-----AKRVVI------DSLS-GLLLA----------LPDPERLREFLH 139

                 ....*..
gi 755495862 423 TLCRKLR 429
Cdd:COG0467  140 RLLRYLK 146
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
595-622 8.32e-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: 8.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 755495862  595 ILLAGPPGCGKTLLAKAVANESGLNFIS 622
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLIS 30
PRK13764 PRK13764
ATPase; Provisional
594-614 8.78e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 39.44  E-value: 8.78e-03
                         10        20
                 ....*....|....*....|.
gi 755495862 594 GILLAGPPGCGKTLLAKAVAN 614
Cdd:PRK13764 259 GILIAGAPGAGKSTFAQALAE 279
PRK04182 PRK04182
cytidylate kinase; Provisional
595-622 9.21e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 37.86  E-value: 9.21e-03
                         10        20
                 ....*....|....*....|....*...
gi 755495862 595 ILLAGPPGCGKTLLAKAVANESGLNFIS 622
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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