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Conserved domains on  [gi|2217267806|ref|XP_047277569|]
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nuclear valosin-containing protein-like isoform X7 [Homo sapiens]

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 ...
125-765 0e+00

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


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 125 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 204 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 283
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 284 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 363
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 364 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 443
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 444 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 523
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 524 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 603
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 604 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 682
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 683 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 755
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 2217267806 756 YERLQESLSR 765
Cdd:TIGR01243 722 YERLAKELKR 731
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
125-765 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 125 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 204 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 283
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 284 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 363
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 364 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 443
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 444 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 523
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 524 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 603
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 604 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 682
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 683 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 755
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 2217267806 756 YERLQESLSR 765
Cdd:TIGR01243 722 YERLAKELKR 731
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
420-751 3.01e-108

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 333.13  E-value: 3.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 420 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 499
Cdd:COG1222    12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 500 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 579
Cdd:COG1222    88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 580 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 658
Cdd:COG1222   168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 659 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 738
Cdd:COG1222   248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                         330
                  ....*....|...
gi 2217267806 739 EAFKKVRSSISKK 751
Cdd:COG1222   312 KAIEKVKKKTETA 324
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
495-655 3.59e-106

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: 321.36  E-value: 3.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 495 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 574
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 575 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                  .
gi 2217267806 655 V 655
Cdd:cd19530   161 V 161
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
485-756 3.30e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 262.08  E-value: 3.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 640
Cdd:PRK03992  206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 641 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 720
Cdd:PRK03992  285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217267806 721 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 756
Cdd:PRK03992  355 ----DDRTE--VTMEDFLKAIEKVMGkeekDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
527-657 4.59e-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: 187.80  E-value: 4.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 606
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217267806 607 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 657
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
485-761 5.57e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.55  E-value: 5.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 636
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 637 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 716
Cdd:NF041006  254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2217267806 717 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 761
Cdd:NF041006  326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
cell_div_CdvC NF041006
cell division protein CdvC;
100-414 5.37e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.17  E-value: 5.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 100 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 174
Cdd:NF041006   66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 175 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 254
Cdd:NF041006  131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 255 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 326
Cdd:NF041006  182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 327 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 406
Cdd:NF041006  259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334

                  ....*...
gi 2217267806 407 KKNPEMED 414
Cdd:NF041006  335 PRPITMED 342
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
523-658 6.49e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.96  E-value: 6.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  523 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 585
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217267806  586 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPgRLDKTLFVGLP 658
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 ...
125-765 0e+00

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 570.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 125 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 203
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 204 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 283
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 284 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 363
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 364 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 443
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 444 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 523
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 524 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 603
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 604 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 682
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 683 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 755
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 2217267806 756 YERLQESLSR 765
Cdd:TIGR01243 722 YERLAKELKR 731
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
420-751 3.01e-108

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 333.13  E-value: 3.01e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 420 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 499
Cdd:COG1222    12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 500 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 579
Cdd:COG1222    88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 580 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 658
Cdd:COG1222   168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 659 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 738
Cdd:COG1222   248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                         330
                  ....*....|...
gi 2217267806 739 EAFKKVRSSISKK 751
Cdd:COG1222   312 KAIEKVKKKTETA 324
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
495-655 3.59e-106

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: 321.36  E-value: 3.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 495 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 574
Cdd:cd19530     1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 575 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19530    81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                  .
gi 2217267806 655 V 655
Cdd:cd19530   161 V 161
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
148-341 6.58e-101

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: 308.18  E-value: 6.58e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppas 226
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAG------------------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 227 asqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 306
Cdd:cd19518    57 ---ELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNN 133
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217267806 307 VA-ATARVLVIGATNRPDSLDPALRRAGRFDREICL 341
Cdd:cd19518   134 EKtAGGPVLVIGATNRPDSLDPALRRAGRFDREICL 169
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
498-655 1.29e-94

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: 291.11  E-value: 1.29e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19511     1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217267806 578 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 655
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
411-745 3.79e-85

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: 275.25  E-value: 3.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 411 EMEDLPSKGVQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREGFVTVPNVTWA 490
Cdd:COG0464    78 LLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:COG0464   158 DLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLD 650
Cdd:COG0464   238 NLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFD 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 651 KTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQemarqksgnekGEL 730
Cdd:COG0464   314 EIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL-----------GRE 377
                         330
                  ....*....|....*
gi 2217267806 731 KVSHKHFEEAFKKVR 745
Cdd:COG0464   378 PVTTEDLLEALERED 392
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
100-395 4.08e-83

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 267.64  E-value: 4.08e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 100 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVV 178
Cdd:COG1222    31 LLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 179 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLREL 258
Cdd:COG1222   111 PPKGVLLYGPPGTGKTLLAKAVAG---------------------------ELGAPFIRVRGSELVSKYIGEGARNVREV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 259 FEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDR 337
Cdd:COG1222   164 FELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATNRPDLLDPALLRPGRFDR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806 338 EICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 395
Cdd:COG1222   241 VIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
485-756 3.30e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 262.08  E-value: 3.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PRK03992  126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 640
Cdd:PRK03992  206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 641 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 720
Cdd:PRK03992  285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217267806 721 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 756
Cdd:PRK03992  355 ----DDRTE--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 ...
148-341 1.52e-72

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: 233.34  E-value: 1.52e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppa 225
Cdd:cd19503     1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVA------------------------ 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 226 sasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLN 305
Cdd:cd19503    56 ---NEAGANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMS 132
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217267806 306 NvaaTARVLVIGATNRPDSLDPALRRAGRFDREICL 341
Cdd:cd19503   133 S---RGKVVVIAATNRPDAIDPALRRPGRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
498-655 1.16e-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: 228.15  E-value: 1.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19529     1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217267806 578 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 655
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 ...
498-655 4.37e-70

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: 227.01  E-value: 4.37e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19528     1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 578 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19528    81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 2217267806 655 V 655
Cdd:cd19528   161 I 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
485-758 5.13e-70

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: 238.34  E-value: 5.13e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRP 636
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 637 DIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRq 716
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVA--RRTPGFSGADLANLLNEAALLAAR- 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2217267806 717 emarqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 758
Cdd:TIGR01241 278 ----------KNKTEITMNDIEEAIDRVIAGPEKKSRVISEK 309
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
491-651 4.51e-69

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: 224.09  E-value: 4.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19503     1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                  .
gi 2217267806 651 K 651
Cdd:cd19503   161 R 161
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
139-415 6.51e-68

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: 229.41  E-value: 6.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 139 FQISNVKFEDVGGNDMTLKEVCKMLIHMRH-PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdf 217
Cdd:COG0464   149 LELREAILDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAG--------------- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 218 sgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQL 297
Cdd:COG0464   214 ------------ELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTL 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 298 LTCMDDLNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPG 377
Cdd:COG0464   282 LTEMEELRS-----DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEG 354
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2217267806 378 FVGADLMALCREAAMCAVnrvlmklqEQQKKNPEMEDL 415
Cdd:COG0464   355 LSGADIRNVVRRAALQAL--------RLGREPVTTEDL 384
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
498-654 3.37e-67

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 218.84  E-value: 3.37e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 498 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19526     1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217267806 578 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19526    81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
485-758 7.99e-66

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 229.15  E-value: 7.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:COG0465   137 PKVTFDDVAGVDEAKEEL-QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLEARQQVFIMAATN 634
Cdd:COG0465   216 VGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGVIVIAATN 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 635 RPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtKpPLDADVNLEAIA----GdlrcdcYTGADLSALVREAS 710
Cdd:COG0465   289 RPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIArrtpG------FSGADLANLVNEAA 359
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2217267806 711 ICAlrqemARqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 758
Cdd:COG0465   360 LLA-----AR------RNKKAVTMEDFEEAIDRVIAGPERKSRVISEK 396
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
494-655 1.10e-61

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: 204.05  E-value: 1.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 494 ALEDIREeltmaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 573
Cdd:cd19481     1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 574 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKT 652
Cdd:cd19481    76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                  ...
gi 2217267806 653 LFV 655
Cdd:cd19481   156 IEF 158
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
148-342 1.35e-61

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: 204.21  E-value: 1.35e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 226
Cdd:cd19519     1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVA------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 227 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNn 306
Cdd:cd19519    56 --NETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK- 132
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217267806 307 vaATARVLVIGATNRPDSLDPALRRAGRFDREICLG 342
Cdd:cd19519   133 --QRAHVIVMAATNRPNSIDPALRRFGRFDREIDIG 166
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
488-651 2.22e-61

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: 203.72  E-value: 2.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 488 TWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 568 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAIL 644
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                  ....*..
gi 2217267806 645 RPGRLDK 651
Cdd:cd19502   161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
487-744 1.36e-60

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 216.07  E-value: 1.36e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 487 VTWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 566
Cdd:CHL00176  180 ITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 567 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLEARQQVFIMAATNRPDI 638
Cdd:CHL00176  259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRVDI 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 639 IDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQEM 718
Cdd:CHL00176  334 LDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARRKK 408
                         250       260
                  ....*....|....*....|....*.
gi 2217267806 719 ArqksgnekgelKVSHKHFEEAFKKV 744
Cdd:CHL00176  409 A-----------TITMKEIDTAIDRV 423
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
124-395 1.50e-60

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 209.30  E-value: 1.50e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 124 IEAVLQKKAKARGLEFQIS---NVKFEDVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAH 198
Cdd:PRK03992  105 IVEVLPSEKDPRVQAMEVIespNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAK 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 199 AIAGAecsgmitAHCSFdfsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAI 278
Cdd:PRK03992  184 AVAHE-------TNATF--------------------IRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 279 TPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQT 355
Cdd:PRK03992  237 AAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---RGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKI 313
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217267806 356 LCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 395
Cdd:PRK03992  314 HTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
487-655 1.44e-59

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: 199.00  E-value: 1.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 487 VTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 566
Cdd:cd19501     1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 567 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAI 643
Cdd:cd19501    80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                         170
                  ....*....|..
gi 2217267806 644 LRPGRLDKTLFV 655
Cdd:cd19501   160 LRPGRFDRQVYV 171
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
498-655 8.39e-59

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 196.58  E-value: 8.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 498 IREELTMAILAPVRNPDQFkALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 577
Cdd:cd19527     1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 578 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-ARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 654
Cdd:cd19527    80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                  .
gi 2217267806 655 V 655
Cdd:cd19527   160 L 160
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
131-397 1.12e-58

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: 207.14  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 131 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 210
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG-------- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 211 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE---VASK 287
Cdd:TIGR01241 111 -------------------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 288 DMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 367
Cdd:TIGR01241 172 DEREQTLNQLLVEMDGFGT---NTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 2217267806 368 FCHLAHLTPGFVGADLMALCREAAMCAVNR 397
Cdd:TIGR01241 249 LKAVARRTPGFSGADLANLLNEAALLAARK 278
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
484-716 3.79e-58

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: 206.10  E-value: 3.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 484 VPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVAN-------ESGLN---FI 553
Cdd:TIGR03689 176 VPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 554 SVKGPELLNMYVGESERAVRQVFQRAKNSA----PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLEAR 624
Cdd:TIGR03689 256 NIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 625 QQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAIL-KTITKNgtkPPLDADvnLEAIAGDlrcdcytgadls 703
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDD---LPLPED--LAAHDGD------------ 394
                         250
                  ....*....|...
gi 2217267806 704 alvREASICALRQ 716
Cdd:TIGR03689 395 ---REATAAALIQ 404
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
470-753 3.82e-58

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 203.07  E-value: 3.82e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 470 SSVQPSAKREGfvtvPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG 549
Cdd:PTZ00454  129 SSIQLLQMSEK----PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTT 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 550 LNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQ 626
Cdd:PTZ00454  205 ATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTN 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 627 VFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAGdlRCDCYTGADLSALV 706
Cdd:PTZ00454  285 VKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAIC 359
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2217267806 707 REASICALRqemarqksgneKGELKVSHKHFEEAFKKVrssISKKDQ 753
Cdd:PTZ00454  360 QEAGMQAVR-----------KNRYVILPKDFEKGYKTV---VRKTDR 392
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
491-656 1.73e-57

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: 193.04  E-value: 1.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19519     1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                  ....*.
gi 2217267806 651 KTLFVG 656
Cdd:cd19519   161 REIDIG 166
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
488-762 1.36e-56

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 204.88  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 488 TWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:PRK10733  150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 568 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLEARQQVFIMAATNRPDII 639
Cdd:PRK10733  229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 640 DPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDlrCDCYTGADLSALVREASICALRqema 719
Cdd:PRK10733  304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2217267806 720 rqksGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQES 762
Cdd:PRK10733  375 ----GNKR---VVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
131-415 1.79e-56

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 203.34  E-value: 1.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 131 KAKARGLEFQISNVKFEDVGGND---MTLKEVCKMLihmRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaEcsg 207
Cdd:COG0465   126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAG-E--- 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 208 mitAHCSFdFSgsndppASASqeldlpilkvaapEIVS---GVsGESeqKLRELFEQAVSNAPCIIFIDEIDAITPKREV 284
Cdd:COG0465   199 ---AGVPF-FS------ISGS-------------DFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGA 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 285 A---SKDmER-RIVAQLLTCMD--DlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 358
Cdd:COG0465   253 GlggGHD-EReQTLNQLLVEMDgfE-----GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHAR 326
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217267806 359 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRvlmklqeqQKKNPEMEDL 415
Cdd:COG0465   327 KKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR--------NKKAVTMEDF 375
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
527-657 4.59e-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: 187.80  E-value: 4.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 606
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217267806 607 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 657
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
146-390 4.54e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 183.93  E-value: 4.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 146 FEDVGGNDmTLKEVCKMLIH-MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndpp 224
Cdd:COG1223     1 LDDVVGQE-EAKKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAG---------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 225 asasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAvSNAPCIIFIDEIDAITPKREVASKDME-RRIVAQLLTCMDD 303
Cdd:COG1223    58 -----ELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 304 LNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADL 383
Cdd:COG1223   132 LPS-----GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADI 204

                  ....*..
gi 2217267806 384 MALCREA 390
Cdd:COG1223   205 EKVLKTA 211
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
496-745 3.00e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 181.62  E-value: 3.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 496 EDIREELTMaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 575
Cdd:COG1223     8 EEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 576 FQRAKNsAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLDKTLF 654
Cdd:COG1223    87 FDFARR-APCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 655 VGLPPPADRLAILKtitKNGTKPPLDADVNLEAIAGdlRCDCYTGADLSALVREasicalrqemARQKSGNEKGElKVSH 734
Cdd:COG1223   162 FPLPDKEERKEILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----------ALKKAILEDRE-KVTK 225
                         250
                  ....*....|.
gi 2217267806 735 KHFEEAFKKVR 745
Cdd:COG1223   226 EDLEEALKQRK 236
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
491-651 1.03e-50

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 174.90  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----EARQQVFIMAATNRPDIIDPAILRP 646
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                  ....*
gi 2217267806 647 GRLDK 651
Cdd:cd19518   161 GRFDR 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
165-339 3.12e-50

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: 172.85  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 165 HMRHPEVyHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIV 244
Cdd:cd19481    12 PRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAG---------------------------ELGLPLIVVKLSSLL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 245 SGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPD 323
Cdd:cd19481    64 SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPD 140
                         170
                  ....*....|....*.
gi 2217267806 324 SLDPALRRAGRFDREI 339
Cdd:cd19481   141 LLDPALLRPGRFDEVI 156
cell_div_CdvC NF041006
cell division protein CdvC;
485-761 5.57e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.55  E-value: 5.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:NF041006   98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 636
Cdd:NF041006  175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 637 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 716
Cdd:NF041006  254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2217267806 717 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 761
Cdd:NF041006  326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
156-339 8.62e-50

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: 171.70  E-value: 8.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 156 LKEVCKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmiTAHCSFdfsgsndppasasqeldl 233
Cdd:cd19511     1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALAS-------EAGLNF------------------ 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 234 piLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATAR 312
Cdd:cd19511    56 --ISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKG 130
                         170       180
                  ....*....|....*....|....*..
gi 2217267806 313 VLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19511   131 VVVIAATNRPDMIDPALLRPGRLDKLI 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
492-655 1.31e-49

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: 171.38  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 492 IGALEDIREELTMAILAPVRNPDQFKaLGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 571
Cdd:cd19509     1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 572 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpgRL 649
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                  ....*.
gi 2217267806 650 DKTLFV 655
Cdd:cd19509   158 EKRIYI 163
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
131-407 6.72e-49

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 182.93  E-value: 6.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 131 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 210
Cdd:PRK10733  136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAG-------- 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 211 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SK 287
Cdd:PRK10733  208 -------------------EAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlggGH 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 288 DMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 367
Cdd:PRK10733  269 DEREQTLNQMLVEMDGFE---GNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDID 345
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2217267806 368 FCHLAHLTPGFVGADLMALCREAAMCAV--NRVLMKLQEQQK 407
Cdd:PRK10733  346 AAIIARGTPGFSGADLANLVNEAALFAArgNKRVVSMVEFEK 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
183-342 2.66e-48

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: 166.61  E-value: 2.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 183 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQA 262
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVA---------------------------KELGAPFIEISGSELVSKYVGESEKRLRELFEAA 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 263 VSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREICLG 342
Cdd:pfam00004  54 KKLAPCVIFIDEIDALAGSRGSGGDSESRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
143-397 9.48e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 171.48  E-value: 9.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 143 NVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsn 221
Cdd:PTZ00454  141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAH---------HTTATF---- 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 222 dppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMER---RIVAQLL 298
Cdd:PTZ00454  208 --------------IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELL 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 299 TCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGF 378
Cdd:PTZ00454  274 NQMDGFDQ---TTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKI 350
                         250
                  ....*....|....*....
gi 2217267806 379 VGADLMALCREAAMCAVNR 397
Cdd:PTZ00454  351 SAADIAAICQEAGMQAVRK 369
ftsH CHL00176
cell division protein; Validated
122-397 1.25e-46

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 176.39  E-value: 1.25e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 122 GEIEAVLQKKAKarglefqiSNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIA 201
Cdd:CHL00176  166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 202 GaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPK 281
Cdd:CHL00176  238 G---------------------------EAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQ 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 282 R--EVASKDMER-RIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 358
Cdd:CHL00176  291 RgaGIGGGNDEReQTLNQLLTEMDGFK---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR 367
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2217267806 359 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNR 397
Cdd:CHL00176  368 NKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARR 406
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
144-339 1.37e-46

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: 163.56  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 144 VKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndp 223
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 224 pasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SKDMERRIVAQLLTC 300
Cdd:cd19501    60 ------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVE 133
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217267806 301 MDDLnnvAATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19501   134 MDGF---ESNTGVIVIAATNRPDVLDPALLRPGRFDRQV 169
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
485-744 2.12e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.49  E-value: 2.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:PTZ00361  178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDP 641
Cdd:PTZ00361  258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 642 AILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRQEmarq 721
Cdd:PTZ00361  338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFI--MAKDELSGADIKAICTEAGLLALRER---- 408
                         250       260
                  ....*....|....*....|...
gi 2217267806 722 ksgnekgELKVSHKHFEEAFKKV 744
Cdd:PTZ00361  409 -------RMKVTQADFRKAKEKV 424
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
146-339 6.76e-46

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: 161.35  E-value: 6.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 146 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndpp 224
Cdd:cd19502     2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVAN---------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 225 asasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDME-RRIVAQLLTCM 301
Cdd:cd19502    60 -----HTDATFIRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQL 134
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2217267806 302 DDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19502   135 DGFD---PRGNIKVIMATNRPDILDPALLRPGRFDRKI 169
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
166-339 3.06e-44

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: 156.50  E-value: 3.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 166 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 245
Cdd:cd19529    13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE--------------SNAN-------------FISVKGPELLS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 246 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDS 324
Cdd:cd19529    66 KWVGESEKAIREIFRKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDI 142
                         170
                  ....*....|....*
gi 2217267806 325 LDPALRRAGRFDREI 339
Cdd:cd19529   143 IDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
146-411 8.37e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 161.09  E-value: 8.37e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 146 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsNDPP 224
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA-------------------NETS 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 225 ASasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 304
Cdd:PTZ00361  243 AT--------FLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQL 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 305 NNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLM 384
Cdd:PTZ00361  315 DGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIK 394
                         250       260
                  ....*....|....*....|....*...
gi 2217267806 385 ALCREAAMCAVNRVLMKL-QEQQKKNPE 411
Cdd:PTZ00361  395 AICTEAGLLALRERRMKVtQADFRKAKE 422
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
491-654 9.10e-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: 152.66  E-value: 9.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 565
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 566 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILR 645
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                  ....*....
gi 2217267806 646 PGRLDKTLF 654
Cdd:cd19517   161 PGRFDREFY 169
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
148-338 1.38e-42

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: 152.28  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGND---MTLKEVckMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgAECSgmitahcsfdfsgsndpp 224
Cdd:cd19517     1 DIGGLShyiNQLKEM--VFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALA-AECS------------------ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 225 aSASQELDLPILKVAapEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 304
Cdd:cd19517    60 -KGGQKVSFFMRKGA--DCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGL 136
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217267806 305 NNvaaTARVLVIGATNRPDSLDPALRRAGRFDRE 338
Cdd:cd19517   137 DN---RGQVVVIGATNRPDALDPALRRPGRFDRE 167
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
485-655 4.08e-42

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 150.78  E-value: 4.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 563
Cdd:cd19521     2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 564 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-EARQQVFIMAATNRPDIIDPA 642
Cdd:cd19521    80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                         170
                  ....*....|...
gi 2217267806 643 ILRpgRLDKTLFV 655
Cdd:cd19521   160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
491-655 5.16e-42

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 150.65  E-value: 5.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALGLVT-PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19520     1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpg 647
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILR-- 158

                  ....*...
gi 2217267806 648 RLDKTLFV 655
Cdd:cd19520   159 RMPKRFHI 166
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
168-339 4.41e-40

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: 144.96  E-value: 4.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 168 HPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGV 247
Cdd:cd19528    15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIAN---------ECQANF------------------ISVKGPELLTMW 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 248 SGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDS 324
Cdd:cd19528    68 FGESEANVRDIFDKARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDI 144
                         170
                  ....*....|....*
gi 2217267806 325 LDPALRRAGRFDREI 339
Cdd:cd19528   145 IDPAILRPGRLDQLI 159
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
491-655 1.11e-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: 143.97  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------EARQQVFIMAATNRPDIIDP 641
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                         170
                  ....*....|....
gi 2217267806 642 AILRpgRLDKTLFV 655
Cdd:cd19522   159 ALRR--RLEKRIYI 170
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
166-337 2.12e-38

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: 140.32  E-value: 2.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 166 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 245
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANE--------------SGAN-------------FISVKGPELLN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 246 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSL 325
Cdd:cd19530    69 KYVGESERAVRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDII 145
                         170
                  ....*....|..
gi 2217267806 326 DPALRRAGRFDR 337
Cdd:cd19530   146 DPAMLRPGRLDK 157
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
167-339 1.03e-36

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 135.25  E-value: 1.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 167 RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahCSFDFsgsndppasasqeldlpiLKVAAPEIVSG 246
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASE---------CGLNF------------------ISVKGPELLNK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 247 VSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLD 326
Cdd:cd19526    67 YIGASEQNVRDLFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLD---GVEGLDGVYVLAATSRPDLID 143
                         170
                  ....*....|...
gi 2217267806 327 PALRRAGRFDREI 339
Cdd:cd19526   144 PALLRPGRLDKLV 156
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
124-353 3.67e-36

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: 143.31  E-value: 3.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 124 IEAVLQKKAKARGLEfQISNVKFEDVGGNDMTLKevckmLIH------MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLA 197
Cdd:TIGR03689 160 FEAIPRTEVEDLVLE-EVPDVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIA 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 198 HAIAGAECSGMitahcsfdFSGSNDPPAsasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNA----PCIIFID 273
Cdd:TIGR03689 234 KAVANSLAARI--------GAEGGGKSY---------FLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFD 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 274 EIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERI 352
Cdd:TIGR03689 297 EMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADI 373

                  .
gi 2217267806 353 L 353
Cdd:TIGR03689 374 F 374
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
485-655 1.04e-35

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: 133.57  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 485 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 564
Cdd:cd19525    17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 565 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPA 642
Cdd:cd19525    96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEA 175
                         170
                  ....*....|...
gi 2217267806 643 ILRpgRLDKTLFV 655
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; ...
513-650 2.82e-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: 131.84  E-value: 2.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 513 PDQFKALGLVTPAGVLLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYVGESERAVRQVF------QRAK- 580
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeeQRRLg 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217267806 581 -NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 650
Cdd:cd19504   100 aNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
cell_div_CdvC NF041006
cell division protein CdvC;
100-414 5.37e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.17  E-value: 5.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 100 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 174
Cdd:NF041006   66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 175 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 254
Cdd:NF041006  131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 255 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 326
Cdd:NF041006  182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 327 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 406
Cdd:NF041006  259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334

                  ....*...
gi 2217267806 407 KKNPEMED 414
Cdd:NF041006  335 PRPITMED 342
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
491-655 1.00e-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: 129.97  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKalGLVTPA-GVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 569
Cdd:cd19524     1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 570 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpg 647
Cdd:cd19524    79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                  ....*...
gi 2217267806 648 RLDKTLFV 655
Cdd:cd19524   157 RFTKRVYV 164
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
149-339 3.67e-34

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: 128.24  E-value: 3.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 149 VGGNDmTLKEVCK--MLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 226
Cdd:cd19509     1 IAGLD-DAKEALKeaVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVA------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 227 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 306
Cdd:cd19509    54 --SESGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN 131
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217267806 307 vAATARVLVIGATNRPDSLDPALRRagRFDREI 339
Cdd:cd19509   132 -KPEDRVLVLGATNRPWELDEAFLR--RFEKRI 161
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
166-337 2.38e-33

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: 125.70  E-value: 2.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 166 MRHPEVYHhLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVS 245
Cdd:cd19527    13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIA---------TECSLNF------------------LSVKGPELIN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 246 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPD 323
Cdd:cd19527    65 MYIGESEANVREVFQKARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPD 142
                         170
                  ....*....|....
gi 2217267806 324 SLDPALRRAGRFDR 337
Cdd:cd19527   143 LLDPALLRPGRFDK 156
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
491-655 4.56e-31

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: 119.40  E-value: 4.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMailapvRNP---DQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 567
Cdd:cd19507     1 DVGGLDNLKDWLKK------RKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 568 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPDIIDPAILRP 646
Cdd:cd19507    75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                  ....*....
gi 2217267806 647 GRLDKTLFV 655
Cdd:cd19507   153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
517-657 1.02e-28

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 112.24  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 517 KALGLVTPAGVLLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFD 590
Cdd:cd00009    12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFID 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217267806 591 EVDALCPRrsdretgASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGL 657
Cdd:cd00009    92 EIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
143-339 8.52e-28

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: 110.34  E-value: 8.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 143 NVKFEDVGGNDMTlKEVCK--MLIHMRHPEVYHHlGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgs 220
Cdd:cd19521     3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVA------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 221 ndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 300
Cdd:cd19521    62 --------TEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQ 133
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217267806 301 MDDLNNvaATARVLVIGATNRPDSLDPALRRagRFDREI 339
Cdd:cd19521   134 MNGVGN--DSQGVLVLGATNIPWQLDSAIRR--RFEKRI 168
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
148-331 7.49e-27

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: 107.51  E-value: 7.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGND---MTLKEvcKMLIHMRHPEVYHHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSFdfsgsndp 223
Cdd:cd19520     1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKE-------AGARF-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 224 pasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDD 303
Cdd:cd19520    64 ------------INLQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDG 131
                         170       180
                  ....*....|....*....|....*...
gi 2217267806 304 LNNvAATARVLVIGATNRPDSLDPALRR 331
Cdd:cd19520   132 LST-DGNCRVIVMGATNRPQDLDEAILR 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
144-339 3.19e-25

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: 103.53  E-value: 3.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 144 VKFEDVGGNDM---TLKEVckMLIHMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgs 220
Cdd:cd19525    19 INWADIAGLEFakkTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIA---------SQSGATF--- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 221 ndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 300
Cdd:cd19525    84 ---------------FSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQ 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217267806 301 MDDLnNVAATARVLVIGATNRPDSLDPALRRagRFDREI 339
Cdd:cd19525   149 LDGA-TTSSEDRILVVGATNRPQEIDEAARR--RLVKRL 184
ycf46 CHL00195
Ycf46; Provisional
430-668 3.85e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 106.64  E-value: 3.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 430 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVA-------LSSVQPSAKRE--------GFV 482
Cdd:CHL00195  144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATyktidenSIPLILEEKKQiisqteilEFY 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 483 TVpNVTWADIGALEDIREELTmailapvRNPDQF--KAL--GLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGP 558
Cdd:CHL00195  222 SV-NEKISDIGGLDNLKDWLK-------KRSTSFskQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 559 ELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPD 637
Cdd:CHL00195  294 KLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATANNID 371
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2217267806 638 IIDPAILRPGRLDKTLFVGLPPPADRLAILK 668
Cdd:CHL00195  372 LLPLEILRKGRFDEIFFLDLPSLEEREKIFK 402
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
179-342 7.42e-24

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: 98.37  E-value: 7.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 179 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasASQELDLPILKVAAPEIVSGVSGESEQK---L 255
Cdd:cd00009    18 PPKNLLLYGPPGTGKTTLARAIAN------------------------ELFRPGAPFLYLNASDLLEGLVVAELFGhflV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 256 RELFEQAVSNAPCIIFIDEIDAITpkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGR 334
Cdd:cd00009    74 RLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDR 142

                  ....*...
gi 2217267806 335 FDREICLG 342
Cdd:cd00009   143 LDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
137-383 8.15e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 105.87  E-value: 8.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 137 LEFQISNVKFEDVGGNDmtlkeVCKMLIHMRH---PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahc 213
Cdd:CHL00195  218 LEFYSVNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIAN----------- 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 214 sfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERR 292
Cdd:CHL00195  282 ----------------DWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNR 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 293 IVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRlP---QAFDFC 369
Cdd:CHL00195  346 VLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIK 419
                         250
                  ....*....|....
gi 2217267806 370 HLAHLTPGFVGADL 383
Cdd:CHL00195  420 KLSKLSNKFSGAEI 433
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
179-339 4.06e-23

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: 96.98  E-value: 4.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 179 PPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLREL 258
Cdd:cd19522    32 PWKGVLMVGPPGTGKTLLAKAVA---------TECGTTF------------------FNVSSSTLTSKYRGESEKLVRLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 259 FEQAVSNAPCIIFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPALRRag 333
Cdd:cd19522    85 FEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEALRR-- 162

                  ....*.
gi 2217267806 334 RFDREI 339
Cdd:cd19522   163 RLEKRI 168
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
176-337 6.60e-23

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: 95.90  E-value: 6.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 176 GVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKL 255
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAG---------------------------VWQLPLLRLDMGRLFGGLVGESESRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 256 RELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGR 334
Cdd:cd19507    80 RQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGR 154

                  ...
gi 2217267806 335 FDR 337
Cdd:cd19507   155 FDE 157
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
169-339 1.62e-22

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: 95.25  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 169 PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIagaecSGMITAhcsfdfsgsNDPPAsasqeldlpilkVAAPEIVSGVS 248
Cdd:cd19504    24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQI-----GKMLNA---------REPKI------------VNGPEILNKYV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 249 GESEQKLRELFEQA---------VSNAPCIIFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNVaatarvL 314
Cdd:cd19504    78 GESEANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNNI------L 150
                         170       180
                  ....*....|....*....|....*
gi 2217267806 315 VIGATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19504   151 VIGMTNRKDLIDEALLRPGRLEVQM 175
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
148-339 1.91e-22

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: 94.53  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgAECSGMItahcsfdfsgsndppas 226
Cdd:cd19524     1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVA-AESNATF----------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 227 asqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 306
Cdd:cd19524    62 ---------FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS 132
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217267806 307 vAATARVLVIGATNRPDSLDPALRRagRFDREI 339
Cdd:cd19524   133 -NGDDRVLVMGATNRPQELDDAVLR--RFTKRV 162
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
491-655 2.51e-21

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: 91.48  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 491 DIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 570
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 571 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpgR 648
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                  ....*..
gi 2217267806 649 LDKTLFV 655
Cdd:cd19523   157 FSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
523-658 6.49e-19

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 83.96  E-value: 6.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  523 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 585
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217267806  586 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPgRLDKTLFVGLP 658
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
179-345 2.07e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.42  E-value: 2.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  179 PPRGVLLHGPPGCGKTLLAHAIAG---AECSGMITAHCSFDFSGsndppasasqeldLPILKVAAPEIVSGVSGESEQKL 255
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEE-------------VLDQLLLIIVGGKKASGSGELRL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  256 RELFEQAVSNAPCIIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRF 335
Cdd:smart00382  68 RLALALARKLKPDVLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RF 138
                          170
                   ....*....|
gi 2217267806  336 DREICLGIPD 345
Cdd:smart00382 139 DRRIVLLLIL 148
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
148-331 1.57e-14

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: 71.84  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 148 DVGGNDM---TLKEvcKMLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndpp 224
Cdd:cd19523     1 DIAGLGAlkaAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLA----------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 225 asasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKReVASKDMERRIVAQLLTCMDDL 304
Cdd:cd19523    55 ----SQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGV 129
                         170       180
                  ....*....|....*....|....*..
gi 2217267806 305 NNvAATARVLVIGATNRPDSLDPALRR 331
Cdd:cd19523   130 LG-SGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
166-339 1.00e-13

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: 69.30  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 166 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAapeiVS 245
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG---------------------------ELDYDICDLN----LS 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 246 GVSGESEQKLRELfeqavSNAP--CIIFIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIG 317
Cdd:cd19510    58 EVVLTDDRLNHLL-----NTAPkqSIILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALD---GVASSEERIVFM 129
                         170       180
                  ....*....|....*....|..
gi 2217267806 318 ATNRPDSLDPALRRAGRFDREI 339
Cdd:cd19510   130 TTNHIERLDPALIRPGRVDMKI 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
510-650 8.06e-13

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: 66.61  E-value: 8.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 510 VRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 588
Cdd:cd19510     9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217267806 589 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGL---EARqqVFIMaATNRPDIIDPAILRPGRLD 650
Cdd:cd19510    81 LEDIDAAFESREHNkknpsAYGGLSRVtFSGLLNALDGVassEER--IVFM-TTNHIERLDPALIRPGRVD 148
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
527-642 1.49e-12

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: 67.09  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 591
Cdd:cd19508    55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217267806 592 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPA 642
Cdd:cd19508   134 VESLAAARSASSSGTepsdAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
527-643 4.04e-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: 61.77  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 605
Cdd:cd19512    25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2217267806 606 ASVR-VVNQLLTEMdGLEARQQVFIMaATNRPDIIDPAI 643
Cdd:cd19512   104 EDLRaALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 140
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
366-405 1.38e-09

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 54.08  E-value: 1.38e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217267806 366 FDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKLQEQ 405
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
519-651 5.80e-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: 55.84  E-value: 5.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 519 LGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 584
Cdd:cd19505     7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217267806 585 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLEARQQVFImAATNRPDIIDPAILRPGRLDK 651
Cdd:cd19505    87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
682-739 4.38e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 49.84  E-value: 4.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806 682 DVNLEAIAGdlRCDCYTGADLSALVREASICALRQEMArqksgnekgelKVSHKHFEE 739
Cdd:pfam17862   1 DVDLEELAE--RTEGFSGADLEALCREAALAALRRGLE-----------AVTQEDLEE 45
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
181-329 6.50e-08

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: 53.60  E-value: 6.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 181 RGVLLHGPPGCGKTLLAHAIAGAecsgmITAHCSFDFSGSNdppasasqeldlpILKVAAPEIVSGVSGESEQKLRELF- 259
Cdd:cd19508    53 RLVLLHGPPGTGKTSLCKALAQK-----LSIRLSSRYRYGQ-------------LIEINSHSLFSKWFSESGKLVTKMFq 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806 260 --EQAVSNAPCIIF--IDEIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 329
Cdd:cd19508   115 kiQELIDDKDALVFvlIDEVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKR---YHNNVILLTSNLLEKIDVAF 189
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
174-339 3.63e-07

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: 50.45  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 174 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMITAhcsfdfsgsndppaSASQELD-LPILKVAAPEIVSGVSGESE 252
Cdd:cd19505     6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRI--------------SLNKLLYnKPDFGNDDWIDGMLILKESL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 253 QKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 331
Cdd:cd19505    72 HRLNLQFELAKAMSPCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIA 151

                  ....*...
gi 2217267806 332 AGRFDREI 339
Cdd:cd19505   152 PNRLDTCI 159
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
528-629 4.65e-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: 53.31  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 528 LLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRRS 600
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY 392
                          90       100
                  ....*....|....*....|....*....
gi 2217267806 601 DRETGASVRVVNQLLTEMDGLEARQQVFI 629
Cdd:TIGR03922 393 GQKDPFGLEAIDTLLARMENDRDRLVVIG 421
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
527-597 5.81e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.39  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 592
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                          90
                  ....*....|
gi 2217267806 593 -----DALCP 597
Cdd:PRK13342  105 nkaqqDALLP 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
527-693 6.89e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.62  E-value: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 598
Cdd:PRK04195   42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 599 RSDReTGAS--VRVVNqlltemdglEARQQVfIMAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--LAILKTITKN- 673
Cdd:PRK04195  113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                         170       180
                  ....*....|....*....|....
gi 2217267806 674 GTKPPLDAdvnLEAIA----GDLR 693
Cdd:PRK04195  177 GIECDDEA---LKEIAersgGDLR 197
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
527-689 7.80e-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: 51.32  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESERAVRQ--VFQRaknsapcVIFFDEVDal 595
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGEFEFRPgpLFAN-------VLLADEIN-- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 596 cprRSDRETGASvrvvnqLLTEMdgleARQQV-------------FIMAATNRPDIID-----PAILRpgRLDKTLFVGL 657
Cdd:COG0714   105 ---RAPPKTQSA------LLEAM----EERQVtipggtyklpepfLVIATQNPIEQEGtyplpEAQLD--RFLLKLYIGY 169
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2217267806 658 PPPADRLAILKTiTKNGTKPPLDADVNLEAIA 689
Cdd:COG0714   170 PDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
527-597 9.28e-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: 9.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFDEV--- 592
Cdd:COG2256    52 MILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVDEIhrf 117
                          90
                  ....*....|
gi 2217267806 593 -----DALCP 597
Cdd:COG2256   118 nkaqqDALLP 127
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
183-275 1.45e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 51.24  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 183 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVsgeseQKLRELFEQA 262
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIA---------------------------GATDAPFEALSA--VTSGV-----KDLREVIEEA 84
                          90
                  ....*....|....*..
gi 2217267806 263 VSNA----PCIIFIDEI 275
Cdd:PRK13342   85 RQRRsagrRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
183-275 3.44e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 50.05  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 183 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVSgeseqKLRELFEQA 262
Cdd:COG2256    52 MILWGPPGTGKTTLARLIA---------------------------NATDAEFVALSA--VTSGVK-----DIREVIEEA 97
                          90
                  ....*....|....*..
gi 2217267806 263 ----VSNAPCIIFIDEI 275
Cdd:COG2256    98 rerrAYGRRTILFVDEI 114
PRK04195 PRK04195
replication factor C large subunit; Provisional
145-202 3.60e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.30  E-value: 3.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806 145 KFEDVGGNDMTLKEVCKMLIHMRHPevyhhlgvVPPRGVLLHGPPGCGKTLLAHAIAG 202
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWIESWLKG--------KPKKALLLYGPPGVGKTSLAHALAN 61
ycf2 CHL00206
Ycf2; Provisional
175-390 6.97e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.91  E-value: 6.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  175 LGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMIT--------------AHCSFDFSGSNDPPASASQELDLPILKVAA 240
Cdd:CHL00206  1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfLIDDIDIDDSDDIDDSDDIDRDLDTELLTM 1704
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806  241 PEIVSG--VSGESEQKLRELFEQAVSNAPCIIFIDEIdaitpkREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGA 318
Cdd:CHL00206  1705 MNALTMdmMPKIDRFYITLQFELAKAMSPCIIWIPNI------HDLNVNESNYLSLGLLVNSLSRDCERCSTRNILVIAS 1778
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806  319 TNRPDSLDPALRRAGRFDREIC---LGIPdeaSRERILQTLCRKLRLPQAFDFCHL---AHLTPGFVGADLMALCREA 390
Cdd:CHL00206  1779 THIPQKVDPALIAPNKLNTCIKirrLLIP---QQRKHFFTLSYTRGFHLEKKMFHTngfGSITMGSNARDLVALTNEA 1853
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
527-560 1.10e-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: 1.10e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
180-305 1.12e-05

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: 46.34  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 180 PRGVLLHGPPGCGKTLLAHAI---AGAECSGMITAHC--------------SFDFSGSNDPPASASQELDLPILKVAAPE 242
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCdenlpyspllealtREGLLRQLLDELESSLLEAWRAALLEALA 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217267806 243 IVSGVSGESEQKLRELFEQAVSNA-----PCIIFIDEIDAItpkrevasKDMERRIVAQLLTCMDDLN 305
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLLDLLargerPLVLVLDDLQWA--------DEASLQLLAALLRLLESLP 163
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
526-645 1.16e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 45.75  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 526 GVLLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 593
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217267806 594 alcprRSDRETgasVRVVNQLLTE-----MDGLE----ARQQVFIMAATNRPDI----IDPAILR 645
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
527-560 3.73e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.66  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
183-391 4.26e-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: 46.31  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 183 VLLHGPPGCGKTLLAHAIAGAecsgmitAHCSF------------DFSGSNDPPASasqeldlpilkvaapeivsgvSGE 250
Cdd:COG0714    34 LLLEGVPGVGKTTLAKALARA-------LGLPFiriqftpdllpsDILGTYIYDQQ---------------------TGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 251 SEQKLRELFEQavsnapcIIFIDEIDAITPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS 324
Cdd:COG0714    86 FEFRPGPLFAN-------VLLADEINRAPPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217267806 325 -----LDPALRRagRFDREICLGIPDEASRERILqtlcrklrlpQAFDFCHLAHLTPGFVGADLMALCREAA 391
Cdd:COG0714   148 egtypLPEAQLD--RFLLKLYIGYPDAEEEREIL----------RRHTGRHLAEVEPVLSPEELLALQELVR 207
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
488-560 4.31e-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: 46.14  E-value: 4.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217267806 488 TWADIGALEDIREELTMAILAPVRNPDQfkalglvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 560
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
526-579 1.04e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217267806 526 GVLLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 579
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
528-593 1.59e-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: 42.93  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 528 LLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIFFDEV 592
Cdd:cd19499    45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVLLDEI 122

                  .
gi 2217267806 593 D 593
Cdd:cd19499   123 E 123
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
527-597 1.72e-04

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: 42.95  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 588
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 2217267806 589 FDEVDALCP 597
Cdd:pfam07724  81 IDEIEKAHP 89
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
497-636 2.31e-04

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


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 42.51  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 497 DIREELTMAILAPVRNPDQFKALGLVTpaGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQ 574
Cdd:cd19506     1 DVRQLLTLYGILPLGSQAVHEKAPLVK--SLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217267806 575 VFQRAKNSAPCVIFFDEVDALCPR---RSDRETGASvRVVNQLLTEMDGLEARQQVFIMAATNRP 636
Cdd:cd19506    79 VLKVARQLQPSVIWIGDAEKTFYKkvpKTEKQLDPK-RLKKDLPKILKSLKPEDRVLIVGTTSRP 142
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
461-598 2.57e-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: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 461 ELNDFIVAlssvQPSAKREGFVTVPNvTWADIGALEDIREEltmailapvrnpdqfkalglVTPAGVLLAGPPGCGKTLL 540
Cdd:cd19498     8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDE--------------------VTPKNILMIGPTGVGKTEI 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217267806 541 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 598
Cdd:cd19498    63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
180-363 2.60e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 43.81  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 180 PRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSfdfsgSNDPPASASQELDLPILKVAAPEivsgvsgeseqkLRELF 259
Cdd:COG0470    18 PHALLLHGPPGIGKTTLALALARD-------LLCE-----NPEGGKACGQCHSRLMAAGNHPD------------LLELN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 260 EQAVSNApciIFIDEIDAITPKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPAL 329
Cdd:COG0470    74 PEEKSDQ---IGIDQIRELGEFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTI 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217267806 330 RragrfdreiclgipdeaSRerilqtlCRKLRLP 363
Cdd:COG0470   149 R-----------------SR-------CQVIRFR 158
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
526-573 2.86e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.19  E-value: 2.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217267806 526 GVLLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 573
Cdd:COG1224    66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
527-558 2.98e-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: 43.53  E-value: 2.98e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217267806 527 VLLAGPPGCGKTLLAKAVANESGLNFISVKGP 558
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
183-201 1.44e-03

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: 39.79  E-value: 1.44e-03
                          10
                  ....*....|....*....
gi 2217267806 183 VLLHGPPGCGKTLLAHAIA 201
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIA 54
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
180-276 1.48e-03

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: 40.24  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 180 PRGVLL-HGPPGCGKTLLAHAIAGAECSG---MITahcsFDFSgsndppaSASQELDLPILKVAAPEIVsgvsGESEQKL 255
Cdd:cd19499    40 PIGSFLfLGPTGVGKTELAKALAELLFGDednLIR----IDMS-------EYMEKHSVSRLIGAPPGYV----GYTEGGQ 104
                          90       100
                  ....*....|....*....|.
gi 2217267806 256 reLFEQAVSNAPCIIFIDEID 276
Cdd:cd19499   105 --LTEAVRRKPYSVVLLDEIE 123
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
180-283 1.55e-03

recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA repair, and the induction of the SOS response. RecA couples ATP hydrolysis to DNA strand exchange.


Pssm-ID: 410863 [Multi-domain]  Cd Length: 235  Bit Score: 41.00  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 180 PRG--VLLHGPPGCGKTLLA-HAIAGAECSGMItahCSF-DFSGSNDPPASASQELDLPILKVAAPEivsgvSGEseQKL 255
Cdd:cd00983    22 PRGriIEIYGPESSGKTTLAlHAIAEAQKLGGT---AAFiDAEHALDPEYAKKLGVDIDNLLVSQPD-----TGE--QAL 91
                          90       100
                  ....*....|....*....|....*....
gi 2217267806 256 rELFEQAV-SNAPCIIFIDEIDAITPKRE 283
Cdd:cd00983    92 -EIADTLIrSGAVDLIVVDSVAALVPKAE 119
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
183-201 2.29e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.83  E-value: 2.29e-03
                          10
                  ....*....|....*....
gi 2217267806 183 VLLHGPPGCGKTLLAHAIA 201
Cdd:COG2255    57 VLLYGPPGLGKTTLAHIIA 75
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
183-201 3.15e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.50  E-value: 3.15e-03
                          10
                  ....*....|....*....
gi 2217267806 183 VLLHGPPGCGKTLLAHAIA 201
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIA 72
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
183-215 3.60e-03

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: 37.58  E-value: 3.60e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217267806 183 VLLHGPPGCGKTLLAHAIAGAECSGMITAHCSF 215
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSV 33
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
527-645 4.08e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.77  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 527 VLLAGPPGCGKTLLAKAVAnesGLNF-----ISVKGPELLNMYVGESERAVRQVFQ------------RAKNSAPCVIFF 589
Cdd:cd00267    28 VALVGPNGSGKSTLLRAIA---GLLKptsgeILIDGKDIAKLPLEELRRRIGYVPQlsggqrqrvalaRALLLNPDLLLL 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217267806 590 DEVD-ALcprrsDRETGASVRvvnQLLTEMdgleARQQVFIMAATNRPDIIDPAILR 645
Cdd:cd00267   105 DEPTsGL-----DPASRERLL---ELLREL----AEEGRTVIIVTHDPELAELAADR 149
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
528-595 4.96e-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: 38.69  E-value: 4.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217267806 528 LLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 595
Cdd:cd19500    41 CLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
183-280 5.02e-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: 38.72  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217267806 183 VLLHGPPGCGKTLLAHAIA---GAECSGMITAHCSfDFSGSNdppaSASQeldlpiLKVAAPEIVSgvSGESEQklreLF 259
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellFGDERALIRIDMS-EYMEEH----SVSR------LIGAPPGYVG--YEEGGQ----LT 68
                          90       100
                  ....*....|....*....|.
gi 2217267806 260 EQAVSNAPCIIFIDEIDAITP 280
Cdd:pfam07724  69 EAVRRKPYSIVLIDEIEKAHP 89
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
531-554 8.26e-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: 37.47  E-value: 8.26e-03
                          10        20
                  ....*....|....*....|....
gi 2217267806 531 GPPGCGKTLLAKAVANESGLNFIS 554
Cdd:cd02020     6 GPAGSGKSTVAKLLAKKLGLPYLD 29
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
526-592 9.88e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 38.61  E-value: 9.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217267806 526 GVLLAGPPGCGKTLLAKAVANE---SGLN--FISVkgPELLN-MYVGESERAVRQVFQRAKnSAPCVIfFDEV 592
Cdd:COG1484   101 NLILLGPPGTGKTHLAIALGHEacrAGYRvrFTTA--PDLVNeLKEARADGRLERLLKRLA-KVDLLI-LDEL 169
 
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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