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Conserved domains on  [gi|1907070075|ref|XP_036009034|]
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nuclear valosin-containing protein-like isoform X3 [Mus musculus]

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 1001098)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
125-738 0e+00

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


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 125 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 204 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 283
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 284 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 363
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 364 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 443
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 444 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 523
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 524 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 602
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 603 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 682
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 683 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 738
Cdd:TIGR01243 669 AMAALRESIGSpakEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELKR 731
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
125-738 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 125 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 204 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 283
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 284 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 363
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 364 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 443
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 444 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 523
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 524 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 602
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 603 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 682
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 683 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 738
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 ...
148-314 2.26e-108

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 326.67  E-value: 2.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 226
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 227 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 305
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                  ....*....
gi 1907070075 306 GRFDREVCL 314
Cdd:cd19518   161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
389-722 4.46e-107

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 329.27  E-value: 4.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 389 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 468
Cdd:COG1222     8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 469 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 548
Cdd:COG1222    84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 549 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:COG1222   164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 628 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 707
Cdd:COG1222   244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                         330
                  ....*....|....*
gi 1907070075 708 KHFEDAFKKVKPSIS 722
Cdd:COG1222   308 EDLEKAIEKVKKKTE 322
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
435-729 2.19e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 2.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 435 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 508
Cdd:PRK03992   98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 509 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 585
Cdd:PRK03992  177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 586 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 664
Cdd:PRK03992  256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 665 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 729
Cdd:PRK03992  333 T--EGASGADLKAICTEAGMFAIRDDRTE-----------VTMEDFLKAIEKVmgkeEKDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
500-630 3.13e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 188.19  E-value: 3.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 579
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 580 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 630
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
458-731 7.38e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 181.86  E-value: 7.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 609
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 610 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 689
Cdd:NF041006  254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907070075 690 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 731
Cdd:NF041006  327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
cell_div_CdvC NF041006
cell division protein CdvC;
143-368 3.84e-37

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.95  E-value: 3.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 143 NVKFEDVGGndatLKEVCKMLIH-----MRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV 217
Cdd:NF041006   99 KVTFSDIVG----LEDVKEALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIM 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 218 SGVSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIG 290
Cdd:NF041006  172 SKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIG 248
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 291 ATNRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 368
Cdd:NF041006  249 ATNKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
496-631 1.79e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075  496 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 558
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075  559 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 631
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
125-738 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 571.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 125 EALLQKKAKARSTELQISNVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGE 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 204 LDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaAT 283
Cdd:TIGR01243 236 AGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLK---GR 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 284 ARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 363
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 364 AMCAVNRVLmkqqAQQKKKPEIEGLPSEgdqeerlgaeptseTQDELQrllgllrdqdplseeqmqglcIELNDFIVALA 443
Cdd:TIGR01243 393 AMAALRRFI----REGKINFEAEEIPAE--------------VLKELK---------------------VTMKDFMEALK 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 444 EVQPSAKREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGL 523
Cdd:TIGR01243 434 MVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGA 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 524 NFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE-TGASVRVVNQLLTEMDGLETRQQVFI 602
Cdd:TIGR01243 514 NFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFdTSVTDRIVNQLLTEMDGIQELSNVVV 593
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 603 LAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREA 682
Cdd:TIGR01243 594 IAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAEDVDLEELAE--MTEGYTGADIEAVCREA 668
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 683 SLCALRQEITA---QKNGVGAGE----LKVSHKHFEDAFKKVKPSISIKDQVMYEALQRSLSQ 738
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 ...
148-314 2.26e-108

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 326.67  E-value: 2.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVCKMLIHM-RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 226
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 227 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVA-ATARVLVIGATNRPDSLDPALRRA 305
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKtAGGPVLVIGATNRPDSLDPALRRA 160

                  ....*....
gi 1907070075 306 GRFDREVCL 314
Cdd:cd19518   161 GRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
389-722 4.46e-107

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 329.27  E-value: 4.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 389 PSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSAKREgfvtVPNVTWADIGAL 468
Cdd:COG1222     8 DENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 469 EDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 548
Cdd:COG1222    84 DEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 549 FQRAKNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:COG1222   164 FELAREKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 628 VGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANDLRcnCYTGADLTALVREASLCALRQEITAqkngvgagelkVSH 707
Cdd:COG1222   244 VPLPDEEAREEILKIHLRD---MPLADDVDLDKLAKLTE--GFSGADLKAIVTEAGMFAIREGRDT-----------VTM 307
                         330
                  ....*....|....*
gi 1907070075 708 KHFEDAFKKVKPSIS 722
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 ...
468-628 9.47e-102

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 309.42  E-value: 9.47e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 468 LEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 547
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 548 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                  .
gi 1907070075 628 V 628
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 ...
471-628 7.06e-92

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 283.41  E-value: 7.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 471 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 550
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 551 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 628
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
136-368 1.44e-88

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 281.12  E-value: 1.44e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 136 STELQISNVKFEDVGGNDATLKEVCKMLI-HMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP 214
Cdd:COG1222    67 AVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 215 EIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATN 293
Cdd:COG1222   147 ELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATN 223
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070075 294 RPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 368
Cdd:COG1222   224 RPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
370-718 8.49e-83

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 268.70  E-value: 8.49e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 370 RVLMKQQAQQKKKPEIEGLPSEGDQEERLGAEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALAEVQPSA 449
Cdd:COG0464    64 ALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 450 KREGFVTVPNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVK 529
Cdd:COG0464   144 LEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVD 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 530 GPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLetRQQVFILAATNRP 609
Cdd:COG0464   224 LSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRP 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 610 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 689
Cdd:COG0464   302 DLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL 374
                         330       340
                  ....*....|....*....|....*....
gi 1907070075 690 eitaqkngvgaGELKVSHKHFEDAFKKVK 718
Cdd:COG0464   375 -----------GREPVTTEDLLEALERED 392
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
435-729 2.19e-78

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 256.68  E-value: 2.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 435 LNDFIVALAEVQPSAKrEGFVTV------PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGC 508
Cdd:PRK03992   98 LNQQSLAIVEVLPSEK-DPRVQAmeviesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGT 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 509 GKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN--- 585
Cdd:PRK03992  177 GKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtl 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 586 -QLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIAND 664
Cdd:PRK03992  256 mQLLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAEL 332
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 665 LrcNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFEDAFKKV----KPSISIKDQVMY 729
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 ...
148-314 3.13e-76

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 242.58  E-value: 3.13e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 225
Cdd:cd19503     1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 226 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRA 305
Cdd:cd19503    80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSS---RGKVVVIAATNRPDAIDPALRRP 156

                  ....*....
gi 1907070075 306 GRFDREVCL 314
Cdd:cd19503   157 GRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
146-368 5.88e-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: 239.81  E-value: 5.88e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 146 FEDVGGNDATLKEVCKMLIHMRH-PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 224
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 225 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRR 304
Cdd:COG0464   236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRS-----DVVVIAATNRPDLLDPALLR 310
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070075 305 agRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 368
Cdd:COG0464   311 --RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQAL 372
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
471-628 4.16e-70

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 226.22  E-value: 4.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 471 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 550
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 551 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFV 628
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 ...
471-628 1.21e-69

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 225.08  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 471 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 550
Cdd:cd19528     1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 551 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 1907070075 628 V 628
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 ...
464-624 5.13e-68

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


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 221.01  E-value: 5.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 543
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 544 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 623
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                  .
gi 1907070075 624 K 624
Cdd:cd19503   161 R 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
458-717 3.35e-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: 229.86  E-value: 3.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRP 609
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 610 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 689
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVAR--RTPGFSGADLANLLNEAALLAARK 278
                         250       260
                  ....*....|....*....|....*...
gi 1907070075 690 EITAqkngvgagelkVSHKHFEDAFKKV 717
Cdd:TIGR01241 279 NKTE-----------ITMNDIEEAIDRV 295
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
148-315 9.52e-67

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 217.69  E-value: 9.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 226
Cdd:cd19519     1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 227 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAG 306
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK---QRAHVIVMAATNRPNSIDPALRRFG 157

                  ....*....
gi 1907070075 307 RFDREVCLG 315
Cdd:cd19519   158 RFDREIDIG 166
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
471-627 1.36e-66

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 216.91  E-value: 1.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 471 IRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 550
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070075 551 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
130-368 8.05e-65

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 220.47  E-value: 8.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 130 KKAKARSTELQIS-NVKFEDVGGNDATLKEVcKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDL 206
Cdd:PRK03992  113 KDPRVQAMEVIESpNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 207 PILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaT 283
Cdd:PRK03992  192 TFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---R 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 284 ARVLVIGATNRPDSLDPALRRAGRFDR--EVCLgiPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCR 361
Cdd:PRK03992  269 GNVKIIAATNRIDILDPAILRPGRFDRiiEVPL--PDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICT 346

                  ....*..
gi 1907070075 362 EAAMCAV 368
Cdd:PRK03992  347 EAGMFAI 353
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-370 4.98e-64

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 221.39  E-value: 4.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 131 KAKARSTELQISNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK 210
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 211 VAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKRE---VASKDMERRIVAQLLTCMDDLNNvaaTARVL 287
Cdd:TIGR01241 119 ISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTLNQLLVEMDGFGT---NTGVI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 288 VIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCA 367
Cdd:TIGR01241 196 VIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275

                  ...
gi 1907070075 368 VNR 370
Cdd:TIGR01241 276 ARK 278
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
467-628 4.06e-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: 204.82  E-value: 4.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 467 ALEDIRDelimaILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 546
Cdd:cd19481     1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 547 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKT 625
Cdd:cd19481    76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                  ...
gi 1907070075 626 LFV 628
Cdd:cd19481   156 IEF 158
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
458-717 6.05e-62

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 217.98  E-value: 6.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADI-GA------LEDIRDELimailapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKG 530
Cdd:COG0465   137 PKVTFDDVaGVdeakeeLQEIVDFL--------KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISG 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 531 PELLNMYVG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLETRQQV 600
Cdd:COG0465   209 SDFVEMFVGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGV 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 601 FILAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtKpPLDEDVNLETIANdlRCNCYTGADLTALVR 680
Cdd:COG0465   282 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIAR--RTPGFSGADLANLVN 356
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907070075 681 EASLCALRqeitaqkngvgAGELKVSHKHFEDAFKKV 717
Cdd:COG0465   357 EAALLAAR-----------RNKKAVTMEDFEEAIDRV 382
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
131-370 3.32e-60

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 212.97  E-value: 3.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 131 KAKARSTELQISNVKFEDVGGND---ATLKEVCKMLihmRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLP 207
Cdd:COG0465   126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 208 ILKVAAPEIVS---GVsGESeqKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDmER-RIVAQLLTCMD--Dln 278
Cdd:COG0465   203 FFSISGSDFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGlggGHD-EReQTLNQLLVEMDgfE-- 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 279 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 358
Cdd:COG0465   277 ---GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLAN 353
                         250
                  ....*....|..
gi 1907070075 359 LCREAAMCAVNR 370
Cdd:COG0465   354 LVNEAALLAARR 365
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
471-628 6.63e-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: 199.28  E-value: 6.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 471 IRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 550
Cdd:cd19527     1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 551 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-TRQQVFILAATNRPDIIDPAILRPGRLDKTLF 627
Cdd:cd19527    80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                  .
gi 1907070075 628 V 628
Cdd:cd19527   160 L 160
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
461-624 6.67e-60

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 199.49  E-value: 6.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 461 TWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 540
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 541 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAIL 617
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                  ....*..
gi 1907070075 618 RPGRLDK 624
Cdd:cd19502   161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
460-717 1.19e-59

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 212.99  E-value: 1.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 460 VTWADIGALEDIRDEL--IMAILapvRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFeeVVSFL---KKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMF 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLETRQQVFILAATNRP 609
Cdd:CHL00176  257 VGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRV 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 610 DIIDPAILRPGRLDKTLFVGLPPPADRVAILKTITKNgtkPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRQ 689
Cdd:CHL00176  332 DILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARR 406
                         250       260
                  ....*....|....*....|....*...
gi 1907070075 690 EITaqkngvgagelKVSHKHFEDAFKKV 717
Cdd:CHL00176  407 KKA-----------TITMKEIDTAIDRV 423
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
460-628 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: 196.30  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 460 VTWADIGALEDIRDELiMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 539
Cdd:cd19501     1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 540 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAI 616
Cdd:cd19501    80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                         170
                  ....*....|..
gi 1907070075 617 LRPGRLDKTLFV 628
Cdd:cd19501   160 LRPGRFDRQVYV 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
146-363 8.69e-58

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 196.64  E-value: 8.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 146 FEDVGGNDATlKEVCKMLIH-MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 224
Cdd:COG1223     1 LDDVVGQEEA-KKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 225 EQKLRELFDQAvSNAPCIVFIDEIDAITPKREVASKDME-RRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALR 303
Cdd:COG1223    80 ARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDGLPS-----GSVVIAATNHPELLDSALW 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 304 RagRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREA 363
Cdd:COG1223   154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
415-655 1.87e-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: 203.79  E-value: 1.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 415 GLLRDQDPLSEEQMQGLCIELndfiVALAEVQPSAKREgfvtVPNVTWADIGAL----EDIRDelimAILAPVRNPDQFR 490
Cdd:TIGR03689 142 EGLRPGDTLLVDPRAGYAFEA----IPRTEVEDLVLEE----VPDVTYADIGGLgsqiEQIRD----AVELPFLHPELYR 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 491 TLGLGTPAGILLAGPPGCGKTLLAKAVAN-------ESGLN---FISVKGPELLNMYVGESERAVRQVFQRAKNSA---- 556
Cdd:TIGR03689 210 EYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegr 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 557 PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGLP 631
Cdd:TIGR03689 290 PVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERP 365
                         250       260
                  ....*....|....*....|....*
gi 1907070075 632 PPADRVAIL-KTITKNgtkPPLDED 655
Cdd:TIGR03689 366 DAEAAADIFaKYLTDD---LPLPED 387
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
458-717 1.87e-56

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 198.06  E-value: 1.87e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:PTZ00454  140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 614
Cdd:PTZ00454  220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 615 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIANdlRCNCYTGADLTALVREASLCALRqeitaq 694
Cdd:PTZ00454  300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAICQEAGMQAVR------ 368
                         250       260
                  ....*....|....*....|...
gi 1907070075 695 KNgvgagELKVSHKHFEDAFKKV 717
Cdd:PTZ00454  369 KN-----RYVILPKDFEKGYKTV 386
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
500-630 3.13e-56

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 188.19  E-value: 3.13e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 579
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 580 SVRVVNQLLTEMDGLETRQQ-VFILAATNRPDIIDPAILrpGRLDKTLFVGL 630
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 ...
464-629 3.85e-56

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 189.18  E-value: 3.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 543
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 544 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 623
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                  ....*.
gi 1907070075 624 KTLFVG 629
Cdd:cd19519   161 REIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
165-312 8.45e-55

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 185.18  E-value: 8.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 165 HMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVF 244
Cdd:cd19481    12 PRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPCILF 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 245 IDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREV 312
Cdd:cd19481    91 IDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPDLLDPALLRPGRFDEVI 156
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
461-735 1.99e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 198.33  E-value: 1.99e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 461 TWADIGALEDIRDElIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 540
Cdd:PRK10733  150 TFADVAGCDEAKEE-VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 541 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLETRQQVFILAATNRPDII 612
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 613 DPAILRPGRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDlrCNCYTGADLTALVREASLCALRqeit 692
Cdd:PRK10733  304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907070075 693 aqkngvgAGELKVSHKHFEDAFKKVKPSISIKDQVMYEALQRS 735
Cdd:PRK10733  375 -------GNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
156-310 4.74e-54

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 183.25  E-value: 4.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 156 LKEVCKMLIHM--RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFD 233
Cdd:cd19511     1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070075 234 QAVSNAPCIVFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
131-367 1.35e-53

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 196.02  E-value: 1.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 131 KAKARS-TELQISNVkFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPIL 209
Cdd:PRK10733  136 KSKARMlTEDQIKTT-FADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFF 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 210 KVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREV---ASKDMERRIVAQLLTCMDDLNnvaATARV 286
Cdd:PRK10733  215 TISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglgGGHDEREQTLNQMLVEMDGFE---GNEGI 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 287 LVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMC 366
Cdd:PRK10733  292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371

                  .
gi 1907070075 367 A 367
Cdd:PRK10733  372 A 372
ftsH CHL00176
cell division protein; Validated
122-370 2.90e-52

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.19  E-value: 2.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 122 GEIEALLQKKAKarstelqiSNVKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIA 201
Cdd:CHL00176  166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 202 GELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDMER-RIVAQLLTCMDDLN 278
Cdd:CHL00176  238 GEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgaGIGGGNDEReQTLNQLLTEMDGFK 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 279 nvaATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMA 358
Cdd:CHL00176  318 ---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLAN 394
                         250
                  ....*....|..
gi 1907070075 359 LCREAAMCAVNR 370
Cdd:CHL00176  395 LLNEAAILTARR 406
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
183-315 3.10e-52

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 177.02  E-value: 3.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDM 262
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 263 ERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREVCLG 315
Cdd:pfam00004  81 SRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
144-312 6.73e-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: 177.81  E-value: 6.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 144 VKFEDVGGNDATLKEVCKMLIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 223
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 224 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVA---SKDMERRIVAQLLTCMDDLnnvAATARVLVIGATNRPDSLDP 300
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVEMDGF---ESNTGVIVIAATNRPDVLDP 157
                         170
                  ....*....|..
gi 1907070075 301 ALRRAGRFDREV 312
Cdd:cd19501   158 ALLRPGRFDRQV 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
479-718 6.68e-51

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 177.77  E-value: 6.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 479 ILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNsAPC 558
Cdd:COG1223    17 IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFARR-APC 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 559 VIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLetRQQVFILAATNRPDIIDPAILRpgRLDKTLFVGLPPPADRV 637
Cdd:COG1223    96 VIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 638 AILKtitKNGTKPPLDEDVNLETIANdlRCNCYTGADLTALVREaslcALRQEITAQKNgvgagelKVSHKHFEDAFKKV 717
Cdd:COG1223   172 EILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----ALKKAILEDRE-------KVTKEDLEEALKQR 235

                  .
gi 1907070075 718 K 718
Cdd:COG1223   236 K 236
cell_div_CdvC NF041006
cell division protein CdvC;
458-731 7.38e-51

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 181.86  E-value: 7.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLETRQQ---VFILAATNRP 609
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 610 DIIDPAILRpgRLDKTLFVGLPPPADRVAILKTITKngtKPPLDEDVNLETIANDLrcNCYTGADLTALVREASLCALRQ 689
Cdd:NF041006  254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVKE 326
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907070075 690 EItaqKNGVGAGElKVSHKHFEDAFKKVKPSIsikDQVM---YEA 731
Cdd:NF041006  327 MF---EKGLGEPR-PITMEDFKEVLKIRKPSV---NQEMlkaYEA 364
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
464-624 2.13e-50

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 173.74  E-value: 2.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 543
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 544 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----ETRQQVFILAATNRPDIIDPAILRP 619
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                  ....*
gi 1907070075 620 GRLDK 624
Cdd:cd19518   161 GRFDR 165
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
465-628 5.18e-50

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 172.54  E-value: 5.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 465 IGALEDIRDELIMAILAPVRNPDQFrTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 544
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 545 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpgRL 622
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                  ....*.
gi 1907070075 623 DKTLFV 628
Cdd:cd19509   158 EKRIYI 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
143-370 1.17e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 179.19  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 143 NVKFEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVS 221
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 222 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMER---RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSL 298
Cdd:PTZ00454  221 GEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQ---TTNVKVIMATNRADTL 297
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 299 DPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAVNR 370
Cdd:PTZ00454  298 DPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
146-312 2.22e-49

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 170.98  E-value: 2.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 146 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 224
Cdd:cd19502     2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 225 EQKLRELFDQAVSNAPCIVFIDEIDAITPKR--EVASKDME-RRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPA 301
Cdd:cd19502    82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFD---PRGNIKVIMATNRPDILDPA 158
                         170
                  ....*....|.
gi 1907070075 302 LRRAGRFDREV 312
Cdd:cd19502   159 LLRPGRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
166-312 5.96e-48

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 166.52  E-value: 5.96e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 166 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 245
Cdd:cd19529    13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKARQVAPCVIFF 92
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070075 246 DEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDSLDPALRRAGRFDREV 312
Cdd:cd19529    93 DEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDIIDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
146-368 5.00e-47

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 173.03  E-value: 5.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 146 FEDVGGNDATLKEVCKML-IHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 224
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 225 EQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 304
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070075 305 AGRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 368
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
458-717 1.85e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.49  E-value: 1.85e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLETRQQVFILAATNRPDIIDP 614
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 615 AILRPGRLDKTLFVGLPPPADRVAILKTITkngTKPPLDEDVNLETIAN---DLrcncyTGADLTALVREASLCALRQEi 691
Cdd:PTZ00361  338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFIMakdEL-----SGADIKAICTEAGLLALRER- 408
                         250       260
                  ....*....|....*....|....*.
gi 1907070075 692 taqkngvgagELKVSHKHFEDAFKKV 717
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 ...
168-310 1.84e-45

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 159.60  E-value: 1.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 168 HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDE 247
Cdd:cd19528    15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARAAAPCVLFFDE 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 248 IDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19528    95 LDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
148-311 2.17e-44

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 157.29  E-value: 2.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVCKM-LIHMRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA-----APEIVSGVS 221
Cdd:cd19517     1 DIGGLSHYINQLKEMvFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 222 GESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPA 301
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDN---RGQVVVIGATNRPDALDPA 157
                         170
                  ....*....|
gi 1907070075 302 LRRAGRFDRE 311
Cdd:cd19517   158 LRRPGRFDRE 167
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
464-627 5.73e-43

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 153.05  E-value: 5.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 538
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 539 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILR 618
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                  ....*....
gi 1907070075 619 PGRLDKTLF 627
Cdd:cd19517   161 PGRFDREFY 169
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
166-310 5.83e-43

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 152.64  E-value: 5.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 166 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 245
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070075 246 DEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19530    96 DEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
458-628 3.32e-42

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 151.17  E-value: 3.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 536
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 537 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-ETRQQVFILAATNRPDIIDPA 615
Cdd:cd19521    80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                         170
                  ....*....|...
gi 1907070075 616 ILRpgRLDKTLFV 628
Cdd:cd19521   160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
464-628 6.57e-42

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 149.88  E-value: 6.57e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLGL-GTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 542
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 543 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpg 620
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTdgNCRVIVMGATNRPQDLDEAILR-- 158

                  ....*...
gi 1907070075 621 RLDKTLFV 628
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 ...
167-312 3.08e-41

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 147.96  E-value: 3.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 167 RHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFID 246
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 247 EIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 312
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 ...
149-312 5.49e-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: 141.72  E-value: 5.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 149 VGGND---ATLKEVckMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESE 225
Cdd:cd19509     1 IAGLDdakEALKEA--VILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 226 QKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRRa 305
Cdd:cd19509    78 KIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN-KPEDRVLVLGATNRPWELDEAFLR- 155

                  ....*..
gi 1907070075 306 gRFDREV 312
Cdd:cd19509   156 -RFEKRI 161
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
464-628 8.02e-39

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 141.66  E-value: 8.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTP-AGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 542
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 543 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------ETRQQVFILAATNRPDIIDP 614
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                         170
                  ....*....|....
gi 1907070075 615 AILRpgRLDKTLFV 628
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 ...
166-310 2.18e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 137.26  E-value: 2.18e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 166 MRHPEVYQhLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFI 245
Cdd:cd19527    13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070075 246 DEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19527    92 DELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPDLLDPALLRPGRFDK 156
cell_div_CdvC NF041006
cell division protein CdvC;
143-368 3.84e-37

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 142.95  E-value: 3.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 143 NVKFEDVGGndatLKEVCKMLIH-----MRHPEVYQhLGVvpPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV 217
Cdd:NF041006   99 KVTFSDIVG----LEDVKEALKEaivypSKRPDLFP-LGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIM 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 218 SGVSGESEQKLRELFDQA-----VSNAPCIVFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIG 290
Cdd:NF041006  172 SKWLGEAEKNVAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIG 248
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 291 ATNRPDSLD-PALRragRFDREVCLGIPDEAARERILQTLCRKLRLPETFNFCHLAHLTPGFVGADLMALCREAAMCAV 368
Cdd:NF041006  249 ATNKPWRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVV 324
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
458-628 9.00e-37

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 136.27  E-value: 9.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 458 PNVTWADIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 537
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 538 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPA 615
Cdd:cd19525    96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTssEDRILVVGATNRPQEIDEA 175
                         170
                  ....*....|...
gi 1907070075 616 ILRpgRLDKTLFV 628
Cdd:cd19525   176 ARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
465-623 2.03e-35

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 132.23  E-value: 2.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 465 IGALE-DIRDELIMAILAPVRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYV 538
Cdd:cd19504     2 IGGLDkEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 539 GESERAVRQVF------QRAK--NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLETRQQVFILAATNR 608
Cdd:cd19504    78 GESEANIRKLFadaeeeQRRLgaNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNR 157
                         170
                  ....*....|....*
gi 1907070075 609 PDIIDPAILRPGRLD 623
Cdd:cd19504   158 KDLIDEALLRPGRLE 172
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
143-326 2.26e-35

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.00  E-value: 2.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 143 NVKFEDVGGNDATLKevckmLIH------MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPI-------- 208
Cdd:TIGR03689 178 DVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIgaegggks 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 209 --LKVAAPEIVSGVSGESEQKLRELFDQAVSNA----PCIVFIDEIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVA 281
Cdd:TIGR03689 253 yfLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVE 329
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1907070075 282 ATARVLVIGATNRPDSLDPALRRAGRFDREVCLGIPDEAARERIL 326
Cdd:TIGR03689 330 SLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIF 374
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
464-628 3.10e-34

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 128.43  E-value: 3.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRtlGLGTPA-GILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 542
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 543 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETR--QQVFILAATNRPDIIDPAILRpg 620
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                  ....*...
gi 1907070075 621 RLDKTLFV 628
Cdd:cd19524   157 RFTKRVYV 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
143-312 3.41e-32

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 122.66  E-value: 3.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 143 NVKFEDVGGNDATlKEVCK--MLIHMRHPEVYQHlGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 220
Cdd:cd19521     3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 221 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDP 300
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGN--DSQGVLVLGATNIPWQLDS 158
                         170
                  ....*....|..
gi 1907070075 301 ALRRagRFDREV 312
Cdd:cd19521   159 AIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
148-304 7.81e-31

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 118.68  E-value: 7.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGND---ATLKEvcKMLIHMRHPEVYQHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGE 223
Cdd:cd19520     1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 224 SEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALR 303
Cdd:cd19520    79 SQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLST-DGNCRVIVMGATNRPQDLDEAIL 157

                  .
gi 1907070075 304 R 304
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; ...
144-304 8.13e-30

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 116.63  E-value: 8.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 144 VKFEDVGGND---ATLKEVckMLIHMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGV 220
Cdd:cd19525    19 INWADIAGLEfakKTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 221 SGESEQKLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLnNVAATARVLVIGATNRPDSLDP 300
Cdd:cd19525    96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGA-TTSSEDRILVVGATNRPQEIDE 174

                  ....
gi 1907070075 301 ALRR 304
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 ...
464-628 1.02e-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: 115.16  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMailapvRNP---DQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 540
Cdd:cd19507     1 DVGGLDNLKDWLKK------RKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 541 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAATNRPDIIDPAILRP 619
Cdd:cd19507    75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                  ....*....
gi 1907070075 620 GRLDKTLFV 628
Cdd:cd19507   153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
494-630 1.41e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 111.85  E-value: 1.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 494 LGTPAGILLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFDEVDA 567
Cdd:cd00009    16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 568 LCPRrsdretgASVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLDKTLFVGL 630
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 ...
176-310 4.52e-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: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 176 GVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPK 254
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNA 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 255 REVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19507   107 DSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
154-304 2.66e-27

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 108.92  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 154 ATLKEVCKML-----IHMRHPEVYQhlGVVPP-RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQK 227
Cdd:cd19522     3 ADLEEAKKLLeeavvLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 228 LRELFDQAVSNAPCIVFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPAL 302
Cdd:cd19522    81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEAL 160

                  ..
gi 1907070075 303 RR 304
Cdd:cd19522   161 RR 162
ycf46 CHL00195
Ycf46; Provisional
142-356 5.33e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 115.50  E-value: 5.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 142 SNVKFEDVGGNDatlkeVCKMLIHMRH---PEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVS 218
Cdd:CHL00195  223 VNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFG 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 219 GVSGESEQKLRELFDQAVSNAPCIVFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDS 297
Cdd:CHL00195  298 GIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNIDL 372
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 298 LDPALRRAGRFDREVCLGIPDEAARERILQTLCRKLRlP---ETFNFCHLAHLTPGFVGADL 356
Cdd:CHL00195  373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIKKLSKLSNKFSGAEI 433
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
148-304 1.27e-26

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 106.47  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGNDATLKEVCKMLI-HMRHPEVYQHLGVvPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGESEQ 226
Cdd:cd19524     1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 227 KLRELFDQAVSNAPCIVFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPA-LRR 304
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS-NGDDRVLVMGATNRPQELDDAvLRR 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
179-315 1.73e-26

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 105.69  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 179 PPRGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSGVSGESEQK---LRELFDQAVSNAPCIVFIDEIDAIT 252
Cdd:cd00009    18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDSLS 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070075 253 pkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGRFDREVCLG 315
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; ...
149-312 1.29e-25

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 104.11  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 149 VGGNDATLKEVCKMLIHMR--HPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILK-VAAPEIVSGVSGESE 225
Cdd:cd19504     2 IGGLDKEFSDIFRRAFASRvfPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVGESE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 226 QKLRELFDQA---------VSNAPCIVFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNvaatarVLVIGA 291
Cdd:cd19504    82 ANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNN------ILVIGM 154
                         170       180
                  ....*....|....*....|.
gi 1907070075 292 TNRPDSLDPALRRAGRFDREV 312
Cdd:cd19504   155 TNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
403-682 5.84e-25

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 109.34  E-value: 5.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 403 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVALAEVQPSA-------KRE--------GFV 455
Cdd:CHL00195  144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATYKTIDENSiplileeKKQiisqteilEFY 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 456 TVpNVTWADIGALEDIRDELimailapvrnpdQFRT---------LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFI 526
Cdd:CHL00195  222 SV-NEKISDIGGLDNLKDWL------------KKRStsfskqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLL 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 527 SVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglETRQQVFILAA 605
Cdd:CHL00195  289 RLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVAT 366
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070075 606 TNRPDIIDPAILRPGRLDKTLFVGLPPPADRVAILKtITKNGTKPPLDEDVNLETIAndLRCNCYTGADLTALVREA 682
Cdd:CHL00195  367 ANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFK-IHLQKFRPKSWKKYDIKKLS--KLSNKFSGAEIEQSIIEA 440
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
464-628 5.13e-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: 87.63  E-value: 5.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 464 DIGALEDIRDELIMAILAPVRNPDQFRTLgLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 543
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 544 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGLET--RQQVFILAATNRPDIIDPAILRpgR 621
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGsgEDGVLVVCTTSKPEEIDESLRR--Y 156

                  ....*..
gi 1907070075 622 LDKTLFV 628
Cdd:cd19523   157 FSKRLLV 163
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
148-304 2.97e-19

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 85.32  E-value: 2.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 148 DVGGND---ATLKEvcKMLIHMRHPEVYQHLgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES 224
Cdd:cd19523     1 DIAGLGalkAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 225 EQKLRELFDQAVSNAPCIVFIDEIDAITPKReVASKDMERRIVAQLLTCMDDLNNvAATARVLVIGATNRPDSLDPALRR 304
Cdd:cd19523    78 EKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGVLG-SGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
496-631 1.79e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075  496 TPAGILLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 558
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075  559 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPgRLDKTLFVGLP 631
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
179-318 1.91e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075  179 PPRGVLLHGPPGCGKTLLAHAIAGELDLPILKV-----------------AAPEIVSGVSGESEQKLRELFDQAVSNAPC 241
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070075  242 IVFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRFDREVCLGIPD 318
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
166-312 2.86e-18

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 82.40  E-value: 2.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 166 MRHPEVYQHLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESEQKLRELfdqavSNAP--CIV 243
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLL-----NTAPkqSII 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070075 244 FIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLDPALRRAGRFDREV 312
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 ...
500-615 2.39e-13

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 69.40  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 564
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907070075 565 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLETRQQVFILAATNRPDIIDPA 615
Cdd:cd19508   134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
483-623 3.22e-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: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 483 VRNPDQFRTLGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 561
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070075 562 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGLETRQQVFILAATNRPDIIDPAILRPGRLD 623
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 ...
500-616 9.23e-12

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 63.31  E-value: 9.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 578
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907070075 579 ASVR-VVNQLLTEMdGLETRQQVFILaATNRPDIIDPAI 616
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 ...
181-312 9.96e-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: 60.62  E-value: 9.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIA--GELDLPILKVA--APEIVSGVSgeseqKLRELFDQA-VSNAPCIVFIDEIDAITPKR 255
Cdd:cd19512    23 RNILFYGPPGTGKTLFAKKLAlhSGMDYAIMTGGdvAPMGREGVT-----AIHKVFDWAnTSRRGLLLFVDEADAFLRKR 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 256 --EVASKDMeRRIVAQLLTCMDDLNNvaataRVLVIGATNRPDSLDPALRraGRFDREV 312
Cdd:cd19512    98 stEKISEDL-RAALNAFLYRTGEQSN-----KFMLVLASNQPEQFDWAIN--DRIDEMV 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
183-248 1.42e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 63.95  E-value: 1.42e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVsgeseQKLRELFDQAVSNA----PCIVFIDEI 248
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; ...
492-624 1.78e-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: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 492 LGLGTPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 557
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 558 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLETRQQVFIlAATNRPDIIDPAILRPGRLDK 624
Cdd:cd19505    87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
183-248 1.81e-10

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 63.54  E-value: 1.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAApeIVSGVSgeseqKLRELFDQA----VSNAPCIVFIDEI 248
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 ...
181-302 5.37e-10

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 59.77  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGELDL---------PILKVAAPEIVSGVSGESEQKLRELFDQA---VSNAPCIVF--ID 246
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIqelIDDKDALVFvlID 132
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 247 EIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 302
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; ...
174-310 1.25e-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: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 174 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVA--------------APEIVSGVSGESEQKLRELFDQAVSNA 239
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070075 240 PCIVFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDR 310
Cdd:cd19505    86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
PRK04195 PRK04195
replication factor C large subunit; Provisional
145-254 2.73e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 60.32  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 145 KFEDVGGNDATLKEVCKMLihmrhpEVYQHlgVVPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAP-----EIVSG 219
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWI------ESWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIER 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907070075 220 VSGESEQKlRELFDQAVSnapcIVFIDEIDAITPK 254
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 ...
339-372 1.03e-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: 1.03e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907070075 339 FNFCHLAHLTPGFVGADLMALCREAAMCAVNRVL 372
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 ...
655-712 3.76e-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: 3.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070075 655 DVNLETIANdlRCNCYTGADLTALVREASLCALRQEITAqkngvgagelkVSHKHFED 712
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 ...
178-308 6.42e-08

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


Pssm-ID: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 53.15  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 178 VPPRGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEI--VSGVSGESEQKLRELFDQavsnapcIVFIDEIDAITPKR 255
Cdd:cd19498    44 VTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVEG-------IVFIDEIDKIAKRG 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 256 EVASKDMERRIVAQLL------TCMDDLNNVAATARVLVIGA----TNRPDSLDPALRraGRF 308
Cdd:cd19498   117 GSSGPDVSREGVQRDLlpivegSTVSTKYGPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
183-364 1.50e-07

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 53.63  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAA-----PEIVSGVS------GESEQKLRELFDQavsnapcIVFIDEIDAI 251
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtpdllPSDILGTYiydqqtGEFEFRPGPLFAN-------VLLADEINRA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 252 TPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS-----LDPALRRagRFDREVCLGIPDEA 320
Cdd:COG0714   107 PPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQegtypLPEAQLD--RFLLKLYIGYPDAE 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907070075 321 ARERILqtlcrKLRLPEtfnfcHLAHLTPGFVGADLMALCREAA 364
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 ...
182-308 4.30e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 182 GVLLHGPPGCGKTLLAHAIAGELD-LPILKVAAP------EIVSGVsgESEQKLRELFDQAVSNA---PCIVFIDEIDAI 251
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQLTrdtteeDLFGRR--NIDPGGASWVDGPLVRAareGEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 252 TPKrevaskdmerrIVAQLLTCMDD----LNN-----VAATARVLVIGATNRPD----SLDPALRRagRF 308
Cdd:pfam07728  79 NPD-----------VLNSLLSLLDErrllLPDggelvKAAPDGFRLIATMNPLDrglnELSPALRS--RF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
500-570 5.78e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 565
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                          90
                  ....*....|
gi 1907070075 566 -----DALCP 570
Cdd:PRK13342  105 nkaqqDALLP 114
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
500-602 6.58e-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: 52.54  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRR 572
Cdd:TIGR03922 315 MLFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETG 391
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907070075 573 SDRETGASVRVVNQLLTEMDGLETRQQVFI 602
Cdd:TIGR03922 392 YGQKDPFGLEAIDTLLARMENDRDRLVVIG 421
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
495-570 8.47e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.98  E-value: 8.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 495 GTPAGILLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFD 563
Cdd:COG2256    47 GRLSSMILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVD 112
                          90
                  ....*....|....*
gi 1907070075 564 EV--------DALCP 570
Cdd:COG2256   113 EIhrfnkaqqDALLP 127
PRK04195 PRK04195
replication factor C large subunit; Provisional
500-666 1.35e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 51.46  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 571
Cdd:PRK04195   42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 572 RSDReTGAS--VRVVNqlltemdglETRQQVfILAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--VAILKTITKN- 646
Cdd:PRK04195  113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                         170       180
                  ....*....|....*....|....
gi 1907070075 647 GTKppLDEDVnLETIAN----DLR 666
Cdd:PRK04195  177 GIE--CDDEA-LKEIAErsggDLR 197
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
181-239 3.30e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 50.35  E-value: 3.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSgvsgeSEQKLRELFDQAVSNA 239
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYS-----AELKKTEFLMQALRKA 120
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
183-256 9.70e-06

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 47.59  E-value: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIV-SGVSGES-EQKLRELFDQA---VSNAP-CIVFIDEIDAITPKRE 256
Cdd:cd19497    53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLLQAAdydVERAQrGIVYIDEIDKIARKSE 132
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
183-308 1.05e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 46.34  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDQAVSNAPC-IVFIDEIDAITPK-REVASK 260
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI---------ERPGDLAAILTNLEPGdVLFIDEIHRLNRAvEEILYP 106
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 261 DMERRivaqlltCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 308
Cdd:pfam05496 107 AMEDF-------RLDIVIGKGPSARSIrldlppftLVGATTRAGLLTSPLR--DRF 153
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
181-312 1.17e-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: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIA------GELDLP-ILKVAAPEIVSGVSGESEQKLRELFDQAVSNapcIVFIDEIDAITP 253
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPlVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070075 254 KREVASKDMERRIVAQLLTCMDDLNNvaataRVLVIGATNRPD-----SLDPALRRagRFDREV 312
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMENDRD-----RLVVIGAGYRKDldkflEVNEGLRS--RFTRVI 446
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
472-662 1.68e-05

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 47.47  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 472 RDELIMAILApvrnpdqfrTLGLGTPagILLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESE 542
Cdd:COG0714    17 QEELIELVLI---------ALLAGGH--LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 543 RAVRQ--VFQRaknsapcVIFFDEVDalcprRSDRETGASvrvvnqLLTEMD------GLETR---QQVFILAATNRPDI 611
Cdd:COG0714    86 FEFRPgpLFAN-------VLLADEIN-----RAPPKTQSA------LLEAMEerqvtiPGGTYklpEPFLVIATQNPIEQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 612 ID-----PAILRpgRLDKTLFVGLPPPADRVAILKTiTKNGTKPPLDEDVNLETIA 662
Cdd:COG0714   148 EGtyplpEAQLD--RFLLKLYIGYPDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
500-533 3.89e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 44.41  E-value: 3.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 533
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
500-570 4.12e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.49  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 561
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 1907070075 562 FDEVDALCP 570
Cdd:pfam07724  81 IDEIEKAHP 89
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
180-303 4.51e-05

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 46.12  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 180 PRGVLLHGPPGCGKTLLAHAIAGEL-------DLPILKVAAPEIVSGVSGEseqkLRELFDQAVSNApcIVfIDEIDAIT 252
Cdd:COG0470    18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGNHPD----LLELNPEEKSDQ--IG-IDQIRELG 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907070075 253 PKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPALR 303
Cdd:COG0470    91 EFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTIR 149
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
181-225 5.72e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 46.15  E-value: 5.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGEL--DLPILKVAAPEIVSGVSGESE 225
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTE 97
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
500-533 7.02e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.51  E-value: 7.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 533
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
183-308 7.87e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 45.37  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELFDqAVSN--APCIVFIDEIDAITPK-REVAS 259
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAA-ILTNleEGDVLFIDEIHRLSPAvEELLY 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070075 260 KDMERrivaqllTCMDDLNNVAATARVL--------VIGATNRPDSLDPALRraGRF 308
Cdd:TIGR00635 103 PAMED-------FRLDIVIGKGPSARSVrldlppftLVGATTRAGMLTSPLR--DRF 150
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
499-552 8.79e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 8.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 499 GILLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 552
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
181-299 8.84e-05

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 43.67  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIVSGVSGES--EQKLRELFDQAVSNAPCIVFIDEIDAI----TPK 254
Cdd:cd19506    27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPK 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907070075 255 REvasKDMERRIVAQLLTCMddLNNVAATARVLVIGATNRPDSLD 299
Cdd:cd19506   107 TE---KQLDPKRLKKDLPKI--LKSLKPEDRVLIVGTTSRPFEAD 146
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
183-253 1.04e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 45.12  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPILKVAAPEIvsgvsgeseQKLRELF---------DqavsnapcIVFIDEIDAITP 253
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL---------EKPGDLAailtnleegD--------VLFIDEIHRLSP 116
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
497-566 1.24e-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: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 497 PAGILLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIF 561
Cdd:cd19499    41 IGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVL 118

                  ....*
gi 1907070075 562 FDEVD 566
Cdd:cd19499   119 LDEIE 123
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
499-618 1.47e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.28  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 499 GILLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 566
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070075 567 alcprRSDRETgasVRVVNQLLTE-----MDGLETRQ----QVFILAATNRPDI----IDPAILR 618
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS 133
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
183-208 1.92e-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: 1.92e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELDLPI 208
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNI 82
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
499-546 2.00e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 499 GILLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 546
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
434-571 2.04e-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: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 434 ELNDFIVAlaevQPSAKREGFVTVPNvTWADIGALEDIRDELimailapvrnpdqfrtlglgTPAGILLAGPPGCGKTLL 513
Cdd:cd19498     8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDEV--------------------TPKNILMIGPTGVGKTEI 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 514 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 571
Cdd:cd19498    63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
500-609 2.39e-04

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 42.13  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQVFQRAKNSAPCVIFFDEVDALCPR---RSD 574
Cdd:cd19506    29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKkvpKTE 108
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907070075 575 RETGASvRVVNQLLTEMDGLETRQQVFILAATNRP 609
Cdd:cd19506   109 KQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
PRK08116 PRK08116
hypothetical protein; Validated
181-250 3.72e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.09  E-value: 3.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVS---GVSGESEQKLRELFDQAVSNAPCIVfIDEIDA 250
Cdd:PRK08116  115 VGLLLWGSVGTGKTYLAACIANELiekGVPVIFVNFPQLLNrikSTYKSSGKEDENEIIRSLVNADLLI-LDDLGA 189
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
183-243 4.11e-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: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELdLPILKVAAPEIVSGVSGE--------------------SEQKLRELFDQAVSNAPCI 242
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARAL-LKKLGLPKDSVYSRNPDDdfwdgytgqpvviiddfgqnPDGPDEAELIRLVSSTPYP 79

                  .
gi 1907070075 243 V 243
Cdd:pfam00910  80 P 80
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
461-533 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: 43.06  E-value: 4.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070075 461 TWADIGALEDIRDELIMAILAPVRNPDQfrtlglgtPAGILLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 533
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
500-531 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 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFISVKGP 531
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
183-299 5.85e-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: 40.18  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVsgvsgeseqkLRELFDQAVSNAPCIVFIDEIDAITPKREVAS 259
Cdd:cd01120     1 ILITGPPGSGKTTLLLQFAEQAllsDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGDR 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907070075 260 KDMERRIVAQLLtcmddlnNVAATARVLVIgATNRPDSLD 299
Cdd:cd01120    71 SSELLEDLAKLL-------RAARNTGITVI-ATIHSDKFD 102
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
184-252 8.21e-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: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 184 LLHGPPGCGKTLLAHAIAGELDLPILKVAapeiVSGVSGESE-----------------QKLRelfdQAVSNAPCIVfID 246
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirghrrtyvgampgriiQALK----KAGTNNPVFL-LD 111

                  ....*.
gi 1907070075 247 EIDAIT 252
Cdd:cd19500   112 EIDKIG 117
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
472-603 1.05e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.56  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 472 RDELIMAILapvrnpDQFRTLGLGTPAGILLAGPPGCGKTLLAKAV---ANESGLNFISVKGPELLNMYVG----ESERA 544
Cdd:pfam13191   5 REEELEQLL------DALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGL 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070075 545 VRQVFQRAKNSAPcVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLETRQQVFIL 603
Cdd:pfam13191  79 LRQLLDELESSLL-EAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
183-253 1.26e-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: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 183 VLLHGPPGCGKTLLAHAIAGELD-----LPI--------------LKVAAPEIVSgvSGESEQklreLFDQAVSNAPCIV 243
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFgderaLIRidmseymeehsvsrLIGAPPGYVG--YEEGGQ----LTEAVRRKPYSIV 79
                          90
                  ....*....|
gi 1907070075 244 FIDEIDAITP 253
Cdd:pfam07724  80 LIDEIEKAHP 89
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
500-568 1.62e-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: 1.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 568
Cdd:cd19500    40 LCLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
181-259 4.87e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.38  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 181 RGVLLHGPPGCGKTLLAHAIAGEL---DLPILKVAAPEIVSG-VSGESEQKLRELFDQaVSNAPCIVfIDEIDAITPKRE 256
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRFTTAPDLVNElKEARADGRLERLLKR-LAKVDLLI-LDELGYLPLDAE 177

                  ...
gi 1907070075 257 VAS 259
Cdd:COG1484   178 GAE 180
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
500-527 5.80e-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: 5.80e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFIS 527
Cdd:cd02020     2 IAIDGPAGSGKSTVAKLLAKKLGLPYLD 29
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
500-527 5.91e-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: 5.91e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFIS 527
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLSLKLIS 30
PRK04182 PRK04182
cytidylate kinase; Provisional
500-527 6.54e-03

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 38.25  E-value: 6.54e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907070075 500 ILLAGPPGCGKTLLAKAVANESGLNFIS 527
Cdd:PRK04182    3 ITISGPPGSGKTTVARLLAEKLGLKHVS 30
PRK13764 PRK13764
ATPase; Provisional
499-519 7.44e-03

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 39.44  E-value: 7.44e-03
                          10        20
                  ....*....|....*....|.
gi 1907070075 499 GILLAGPPGCGKTLLAKAVAN 519
Cdd:PRK13764  259 GILIAGAPGAGKSTFAQALAE 279
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
180-334 8.32e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.36  E-value: 8.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 180 PRG--VLLHGPPGCGKTLLAHAIAGELdlpilkVAAPE---IVSgvSGESEQKLREL-------FDQAVSNApCIVFIDe 247
Cdd:COG0467    18 PRGssTLLSGPPGTGKTTLALQFLAEG------LRRGEkglYVS--FEESPEQLLRRaeslgldLEEYIESG-LLRIID- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070075 248 idaITPKREVASKDMerrIVAQLLTCMDDLNnvaatARVLVIgatnrpDSLDpALRRAgrfdrevclgIPDEAARERILQ 327
Cdd:COG0467    88 ---LSPEELGLDLEE---LLARLREAVEEFG-----AKRVVI------DSLS-GLLLA----------LPDPERLREFLH 139

                  ....*..
gi 1907070075 328 TLCRKLR 334
Cdd:COG0467   140 RLLRYLK 146
 
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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