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Conserved domains on  [gi|341865579|ref|NP_001230075|]
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nuclear valosin-containing protein-like isoform 3 [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 ...
27-667 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: 567.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   27 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 105
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  106 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 185
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  186 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 265
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  266 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 345
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  346 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 425
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  426 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 505
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  506 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 584
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  585 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 657
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 341865579  658 YERLQESLSR 667
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 ...
27-667 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: 567.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   27 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 105
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  106 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 185
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  186 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 265
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  266 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 345
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  346 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 425
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  426 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 505
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  506 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 584
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  585 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 657
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 341865579  658 YERLQESLSR 667
Cdd:TIGR01243 722 YERLAKELKR 731
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
322-653 3.96e-108

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 330.04  E-value: 3.96e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 322 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 401
Cdd:COG1222   12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 402 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 481
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 482 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 560
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 561 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 640
Cdd:COG1222  248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                        330
                 ....*....|...
gi 341865579 641 EAFKKVRSSISKK 653
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 ...
397-557 2.09e-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: 319.43  E-value: 2.09e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 397 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 476
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 477 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 556
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 341865579 557 V 557
Cdd:cd19530  161 V 161
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
387-658 1.61e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 260.53  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 542
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 543 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 622
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 341865579 623 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 658
Cdd:PRK03992 355 ----DDRTE--VTMEDFLKAIEKVMGkeekDSMEEPGVMF 388
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
429-559 2.60e-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: 187.03  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 508
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341865579  509 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 559
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
387-663 1.88e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.55  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 538
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 539 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 618
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 341865579 619 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 663
Cdd:NF041006 326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
cell_div_CdvC NF041006
cell division protein CdvC;
2-316 3.42e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.17  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   2 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 76
Cdd:NF041006  66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  77 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 156
Cdd:NF041006 131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 157 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 228
Cdd:NF041006 182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 229 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 308
Cdd:NF041006 259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334

                 ....*...
gi 341865579 309 KKNPEMED 316
Cdd:NF041006 335 PRPITMED 342
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
425-560 1.64e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   425 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 487
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865579   488 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPgRLDKTLFVGLP 560
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 ...
27-667 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: 567.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   27 EAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAga 105
Cdd:TIGR01243 156 EVEIREKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVeLPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVA-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  106 ecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE 185
Cdd:TIGR01243 234 -------------------------NEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKRE 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  186 VASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLP 265
Cdd:TIGR01243 289 EVTGEVEKRVVAQLLTLMDGLK---GRGRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLA 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  266 QAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLmklqEQQKKNPEMEDLPSkgvqeerlgteptsETQDELQrllgl 345
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFI----REGKINFEAEEIPA--------------EVLKELK----- 422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  346 lrdqdplseeqmqglcIELNDFIVALSSVQPSAKREGFVTVPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVT 425
Cdd:TIGR01243 423 ----------------VTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRP 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  426 PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRE 505
Cdd:TIGR01243 487 PKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARF 566
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  506 -TGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDAD 584
Cdd:TIGR01243 567 dTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTR---SMPLAED 643
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  585 VNLEAIAGdlRCDCYTGADLSALVREASICALRQEM---ARQKSGNEKGE----LKVSHKHFEEAFKKVRSSISKKDQIM 657
Cdd:TIGR01243 644 VDLEELAE--MTEGYTGADIEAVCREAAMAALRESIgspAKEKLEVGEEEflkdLKVEMRHFLEALKKVKPSVSKEDMLR 721
                         650
                  ....*....|
gi 341865579  658 YERLQESLSR 667
Cdd:TIGR01243 722 YERLAKELKR 731
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
322-653 3.96e-108

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 330.04  E-value: 3.96e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 322 VQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREgfvtVPNVTWADIGALEDIR 401
Cdd:COG1222   12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAE----SPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 402 EELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRA 481
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 482 KNSAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLP 560
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDdGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 561 PPADRLAILKTITKNgtkPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRQEMARqksgnekgelkVSHKHFE 640
Cdd:COG1222  248 DEEAREEILKIHLRD---MPLADDVDLDKLAKLT--EGFSGADLKAIVTEAGMFAIREGRDT-----------VTMEDLE 311
                        330
                 ....*....|...
gi 341865579 641 EAFKKVRSSISKK 653
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 ...
397-557 2.09e-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: 319.43  E-value: 2.09e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 397 LEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQ 476
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 477 VFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 556
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                 .
gi 341865579 557 V 557
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 ...
50-243 1.97e-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: 306.64  E-value: 1.97e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGNDMTLKEVCKMLIHM-RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppas 128
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPiLPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAG------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 129 asqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 208
Cdd:cd19518   57 ---ELKVPFLKISATEIVSGVSGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNN 133
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 341865579 209 VA-ATARVLVIGATNRPDSLDPALRRAGRFDREICL 243
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 ...
400-557 3.68e-95

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: 289.95  E-value: 3.68e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 400 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 479
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865579 480 RAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 557
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSdSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
313-647 8.12e-84

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 269.47  E-value: 8.12e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 313 EMEDLPSKGVQEERLGTEPTSETQDELQRLLGLLRDQDPLSEEQMQGLCIELNDFIVALSSVQPSAKREGFVTVPNVTWA 392
Cdd:COG0464   78 LLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILD 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 472
Cdd:COG0464  158 DLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEK 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 473 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLD 552
Cdd:COG0464  238 NLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFD 313
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 553 KTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQemarqksgnekGEL 632
Cdd:COG0464  314 EIIFFPLPDAEERLEIFRIHLR---KRPLDEDVDLEELAE--ATEGLSGADIRNVVRRAALQALRL-----------GRE 377
                        330
                 ....*....|....*
gi 341865579 633 KVSHKHFEEAFKKVR 647
Cdd:COG0464  378 PVTTEDLLEALERED 392
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
2-297 4.67e-83

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 264.95  E-value: 4.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   2 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVV 80
Cdd:COG1222   31 LLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVElPLKNPELFRKYGIE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  81 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLREL 160
Cdd:COG1222  111 PPKGVLLYGPPGTGKTLLAKAVAG---------------------------ELGAPFIRVRGSELVSKYIGEGARNVREV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 161 FEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDR 239
Cdd:COG1222  164 FELAREKAPSIIFIDEIDAIAARRtDDGTSGEVQRTVNQLLAELDGFES---RGDVLIIAATNRPDLLDPALLRPGRFDR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579 240 EICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 297
Cdd:COG1222  241 VIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAI 298
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
387-658 1.61e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 260.53  E-value: 1.61e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVN----QLLTEMDGLEARQQVFIMAATNRPDIID 542
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 543 PAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRqemar 622
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR---KMNLADDVDLEELAELT--EGASGADLKAICTEAGMFAIR----- 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 341865579 623 qksgNEKGElkVSHKHFEEAFKKVRS----SISKKDQIMY 658
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 ...
50-243 1.50e-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: 231.41  E-value: 1.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppa 127
Cdd:cd19503    1 DIGGLDEQIASL-KELIELplKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVA------------------------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 128 sasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLN 207
Cdd:cd19503   56 ---NEAGANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMS 132
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 341865579 208 NvaaTARVLVIGATNRPDSLDPALRRAGRFDREICL 243
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 ...
400-557 3.89e-71

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 227.76  E-value: 3.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 400 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 479
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 341865579 480 RAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFV 557
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 ...
400-557 7.34e-71

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: 7.34e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 400 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 479
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 480 RAKNSAPCVIFFDEVDALCPRRS---DRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 556
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 341865579 557 V 557
Cdd:cd19528  161 I 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
387-660 3.73e-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: 236.41  E-value: 3.73e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  387 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  467 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRP 538
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggnDERE-----QTLNQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  539 DIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRq 618
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKN---KKLAPDVDLKAVA--RRTPGFSGADLANLLNEAALLAAR- 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 341865579  619 emarqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 660
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 ...
393-553 3.86e-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: 222.55  E-value: 3.86e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 472
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 473 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 552
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 .
gi 341865579 553 K 553
Cdd:cd19503  161 R 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
400-556 7.26e-68

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: 7.26e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 400 IREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 479
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865579 480 RAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 556
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
41-317 1.07e-66

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: 224.40  E-value: 1.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  41 FQISNVKFEDVGGNDMTLKEVCKMLIHMRH-PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdf 119
Cdd:COG0464  149 LELREAILDDLGGLEEVKEELRELVALPLKrPELREEYGLPPPRGLLLYGPPGTGKTLLARALAG--------------- 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 120 sgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQL 199
Cdd:COG0464  214 ------------ELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTL 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 200 LTCMDDLNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPG 279
Cdd:COG0464  282 LTEMEELRS-----DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEG 354
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 341865579 280 FVGADLMALCREAAMCAVnrvlmklqEQQKKNPEMEDL 317
Cdd:COG0464  355 LSGADIRNVVRRAALQAL--------RLGREPVTTEDL 384
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
387-660 1.15e-65

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 226.46  E-value: 1.15e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:COG0465  137 PKVTFDDVAGVDEAKEEL-QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VG--ESeRaVRQVFQRAKNSAPCVIFFDEVDALCPRRS--------DREtgasvRVVNQLLTEMDGLEARQQVFIMAATN 536
Cdd:COG0465  216 VGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglggghdERE-----QTLNQLLVEMDGFEGNEGVIVIAATN 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 537 RPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtKpPLDADVNLEAIA----GdlrcdcYTGADLSALVREAS 612
Cdd:COG0465  289 RPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK--K-PLAPDVDLEVIArrtpG------FSGADLANLVNEAA 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 341865579 613 ICAlrqemARqksgneKGELKVSHKHFEEAFKKVRSSISKKDQIMYER 660
Cdd:COG0465  360 LLA-----AR------RNKKAVTMEDFEEAIDRVIAGPERKSRVISEK 396
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
50-244 4.93e-62

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: 203.82  E-value: 4.93e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 128
Cdd:cd19519    1 DIGGCRKQLAQIREMVeLPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVA------------------------- 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 129 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNn 208
Cdd:cd19519   56 --NETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLK- 132
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 341865579 209 vaATARVLVIGATNRPDSLDPALRRAGRFDREICLG 244
Cdd:cd19519  133 --QRAHVIVMAATNRPNSIDPALRRFGRFDREIDIG 166
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
396-557 1.21e-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: 202.51  E-value: 1.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 396 ALEDIREeltmaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVR 475
Cdd:cd19481    1 LKASLRE-----AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 476 QVFQRAKNSAPCVIFFDEVDALCPRRSDR-ETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKT 554
Cdd:cd19481   76 KIFERARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                 ...
gi 341865579 555 LFV 557
Cdd:cd19481  156 IEF 158
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
390-553 1.54e-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: 202.57  E-value: 1.54e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 390 TWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 469
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 470 SERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAIL 546
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                 ....*..
gi 341865579 547 RPGRLDK 553
Cdd:cd19502  161 RPGRFDR 167
ftsH CHL00176
cell division protein; Validated
389-646 2.34e-61

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 216.07  E-value: 2.34e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 389 VTWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 468
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 469 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRR--------SDRETgasvrVVNQLLTEMDGLEARQQVFIMAATNRPDI 540
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRgagigggnDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRVDI 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 541 IDPAILRPGRLDKTLFVGLPPPADRLAILKTITKNgtkPPLDADVNLEAIAGdlRCDCYTGADLSALVREASICALRQEM 620
Cdd:CHL00176 334 LDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARRKK 408
                        250       260
                 ....*....|....*....|....*.
gi 341865579 621 ArqksgnekgelKVSHKHFEEAFKKV 646
Cdd:CHL00176 409 A-----------TITMKEIDTAIDRV 423
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
26-297 9.83e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 208.15  E-value: 9.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  26 IEAVLQKKAKARGLEFQIS---NVKFEDVGGNDMTLKEVcKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAH 100
Cdd:PRK03992 105 IVEVLPSEKDPRVQAMEVIespNVTYEDIGGLEEQIREV-REAVELplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 101 AIAGAecsgmitAHCSFdfsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAI 180
Cdd:PRK03992 184 AVAHE-------TNATF--------------------IRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAI 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 181 TPKR--EVASKDME-RRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQT 257
Cdd:PRK03992 237 AAKRtdSGTSGDREvQRTLMQLLAEMDGFDP---RGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKI 313
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 341865579 258 LCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAV 297
Cdd:PRK03992 314 HTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAI 353
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
400-557 1.52e-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: 196.97  E-value: 1.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 400 IREELTMAILAPVRNPDQFkALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQ 479
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 480 RAKNSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLE-ARQQVFIMAATNRPDIIDPAILRPGRLDKTLF 556
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVmdRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                 .
gi 341865579 557 V 557
Cdd:cd19527  160 L 160
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
389-557 1.64e-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: 197.07  E-value: 1.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 389 VTWADIGALEDIREELtMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVG 468
Cdd:cd19501    1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 469 ESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASV---RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAI 545
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 341865579 546 LRPGRLDKTLFV 557
Cdd:cd19501  160 LRPGRFDRQVYV 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
372-655 9.28e-59

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 203.07  E-value: 9.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 372 SSVQPSAKREGfvtvPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG 451
Cdd:PTZ00454 129 SSIQLLQMSEK----PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTT 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 452 LNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQ 528
Cdd:PTZ00454 205 ATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADrevQRILLELLNQMDGFDQTTN 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 529 VFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAGdlRCDCYTGADLSALV 608
Cdd:PTZ00454 285 VKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTIT---SKMNLSEEVDLEDFVS--RPEKISAADIAAIC 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 341865579 609 REASICALRqemarqksgneKGELKVSHKHFEEAFKKVrssISKKDQ 655
Cdd:PTZ00454 360 QEAGMQAVR-----------KNRYVILPKDFEKGYKTV---VRKTDR 392
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
33-299 1.00e-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: 205.60  E-value: 1.00e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   33 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 112
Cdd:TIGR01241  39 KSKAKLLNEEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG-------- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  113 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE---VASK 189
Cdd:TIGR01241 111 -------------------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  190 DMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 269
Cdd:TIGR01241 172 DEREQTLNQLLVEMDGFGT---NTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 341865579  270 FCHLAHLTPGFVGADLMALCREAAMCAVNR 299
Cdd:TIGR01241 249 LKAVARRTPGFSGADLANLLNEAALLAARK 278
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
386-618 5.23e-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: 204.17  E-value: 5.23e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  386 VPNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVAN-------ESGLN---FI 455
Cdd:TIGR03689 176 VPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANslaarigAEGGGksyFL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  456 SVKGPELLNMYVGESERAVRQVFQRAKNSA----PCVIFFDEVDALCPRR-----SDRETgasvRVVNQLLTEMDGLEAR 526
Cdd:TIGR03689 256 NIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRgsgvsSDVET----TVVPQLLAEIDGVESL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  527 QQVFIMAATNRPDIIDPAILRPGRLDKTLFVGLPPPADRLAIL-KTITKNgtkPPLDADvnLEAIAGDlrcdcytgadls 605
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDD---LPLPED--LAAHDGD------------ 394
                         250
                  ....*....|...
gi 341865579  606 alvREASICALRQ 618
Cdd:TIGR03689 395 ---REATAAALIQ 404
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
393-558 6.97e-58

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: 192.65  E-value: 6.97e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 472
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 473 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 552
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 341865579 553 KTLFVG 558
Cdd:cd19519  161 REIDIG 166
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
390-664 3.24e-57

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 204.88  E-value: 3.24e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 390 TWADIGALEDIREELTmAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 469
Cdd:PRK10733 150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 470 SERAVRQVFQRAKNSAPCVIFFDEVDALcprrsDRETGASV--------RVVNQLLTEMDGLEARQQVFIMAATNRPDII 541
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAV-----GRQRGAGLggghdereQTLNQMLVEMDGFEGNEGIIVIAATNRPDVL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 542 DPAILRPGRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDlrCDCYTGADLSALVREASICALRqema 621
Cdd:PRK10733 304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMR---RVPLAPDIDAAIIARG--TPGFSGADLANLVNEAALFAAR---- 374
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 341865579 622 rqksGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQES 664
Cdd:PRK10733 375 ----GNKR---VVSMVEFEKAKDKIMMGAERRSMVMTEAQKES 410
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
429-559 2.60e-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: 187.03  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGA 508
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341865579  509 SVRVVNQLLTEMDGLEARQQ-VFIMAATNRPDIIDPAILrpGRLDKTLFVGL 559
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
33-317 3.41e-56

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 200.65  E-value: 3.41e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  33 KAKARGLEFQISNVKFEDVGGND---MTLKEVCKMLihmRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaEcsg 109
Cdd:COG0465  126 KSKAKLYDEDKPKVTFDDVAGVDeakEELQEIVDFL---KDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAG-E--- 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 110 mitAHCSFdFSgsndppASASqeldlpilkvaapEIVS---GVsGESeqKLRELFEQAVSNAPCIIFIDEIDAITPKREV 186
Cdd:COG0465  199 ---AGVPF-FS------ISGS-------------DFVEmfvGV-GAS--RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGA 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 187 A---SKDmER-RIVAQLLTCMD--DlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 260
Cdd:COG0465  253 GlggGHD-EReQTLNQLLVEMDgfE-----GNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHAR 326
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 341865579 261 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNRvlmklqeqQKKNPEMEDL 317
Cdd:COG0465  327 KKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARR--------NKKAVTMEDF 375
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
48-292 5.54e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 182.39  E-value: 5.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  48 FEDVGGNDmTLKEVCKMLIH-MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndpp 126
Cdd:COG1223    1 LDDVVGQE-EAKKKLKLIIKeLRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAG---------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 127 asasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAvSNAPCIIFIDEIDAITPKREVASKDME-RRIVAQLLTCMDD 205
Cdd:COG1223   58 -----ELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEvKRVVNALLQELDG 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 206 LNNvaataRVLVIGATNRPDSLDPALRRagRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADL 285
Cdd:COG1223  132 LPS-----GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADI 204

                 ....*..
gi 341865579 286 MALCREA 292
Cdd:COG1223  205 EKVLKTA 211
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
398-647 3.59e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 180.46  E-value: 3.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 398 EDIREELTMaILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERAVRQV 477
Cdd:COG1223    8 EEAKKKLKL-IIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 478 FQRAKNsAPCVIFFDEVDALCPRRSD-RETGASVRVVNQLLTEMDGLeaRQQVFIMAATNRPDIIDPAILRpgRLDKTLF 556
Cdd:COG1223   87 FDFARR-APCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR--RFDEVIE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 557 VGLPPPADRLAILKtitKNGTKPPLDADVNLEAIAGdlRCDCYTGADLSALVREasicalrqemARQKSGNEKGElKVSH 636
Cdd:COG1223  162 FPLPDKEERKEILE---LNLKKFPLPFELDLKKLAK--KLEGLSGADIEKVLKT----------ALKKAILEDRE-KVTK 225
                        250
                 ....*....|.
gi 341865579 637 KHFEEAFKKVR 647
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 ...
393-553 6.95e-51

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: 174.13  E-value: 6.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 472
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 473 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL----EARQQVFIMAATNRPDIIDPAILRP 548
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*
gi 341865579 549 GRLDK 553
Cdd:cd19518  161 GRFDR 165
cell_div_CdvC NF041006
cell division protein CdvC;
387-663 1.88e-50

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 179.55  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFkALGLvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSA-----PCVIFFDEVDALCPRRSDrETGASVRVVNQLLTEMDGLEARQQ---VFIMAATNRP 538
Cdd:NF041006 175 LGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSS-EVGGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 539 DIIDPAILRpgRLDKTLFVGLPPPADRLAILKTITKngtKPPLDADVNLEAIAGDLrcDCYTGADLSALVREASICALRq 618
Cdd:NF041006 254 WRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS---KIKLENDVDLDELAEMT--EGYTASDIRDIVQAAHMRVVK- 325
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 341865579 619 EMARQKSGNEKgelKVSHKHFEEAFKKVRSSISKKDQIMYERLQE 663
Cdd:NF041006 326 EMFEKGLGEPR---PITMEDFKEVLKIRKPSVNQEMLKAYEAWHE 367
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
394-557 3.89e-50

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 171.77  E-value: 3.89e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 394 IGALEDIREELTMAILAPVRNPDQFKaLGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESERA 473
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFP-GLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 474 VRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpgRL 551
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 341865579 552 DKTLFV 557
Cdd:cd19509  158 EKRIYI 163
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
67-241 4.88e-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: 171.31  E-value: 4.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  67 HMRHPEVyHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIV 146
Cdd:cd19481   12 PRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAG---------------------------ELGLPLIVVKLSSLL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 147 SGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKRE-VASKDMERRIVAQLLTCMDDLNNvaaTARVLVIGATNRPD 225
Cdd:cd19481   64 SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNS---RSKVLVIAATNRPD 140
                        170
                 ....*....|....*.
gi 341865579 226 SLDPALRRAGRFDREI 241
Cdd:cd19481  141 LLDPALLRPGRFDEVI 156
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
58-241 6.31e-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: 170.93  E-value: 6.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  58 LKEVCKMLIHM--RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmiTAHCSFdfsgsndppasasqeldl 135
Cdd:cd19511    1 VKRELKEAVEWplKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALAS-------EAGLNF------------------ 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 136 piLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDdlnNVAATAR 214
Cdd:cd19511   56 --ISVKGPELFSKYVGESERAVREIFQKARQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELD---GIESLKG 130
                        170       180
                 ....*....|....*....|....*..
gi 341865579 215 VLVIGATNRPDSLDPALRRAGRFDREI 241
Cdd:cd19511  131 VVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
33-309 2.24e-49

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 182.93  E-value: 2.24e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  33 KAKARGLEFQISNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmit 112
Cdd:PRK10733 136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAG-------- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 113 ahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SK 189
Cdd:PRK10733 208 -------------------EAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGlggGH 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 190 DMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFD 269
Cdd:PRK10733 269 DEREQTLNQMLVEMDGFE---GNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDID 345
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 341865579 270 FCHLAHLTPGFVGADLMALCREAAMCAV--NRVLMKLQEQQK 309
Cdd:PRK10733 346 AAIIARGTPGFSGADLANLVNEAALFAArgNKRVVSMVEFEK 387
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
85-244 1.81e-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: 166.23  E-value: 1.81e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   85 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQA 164
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVA---------------------------KELGAPFIEISGSELVSKYVGESEKRLRELFEAA 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  165 VSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPDSLDPALRraGRFDREICLG 244
Cdd:pfam00004  54 KKLAPCVIFIDEIDALAGSRGSGGDSESRRVVNQLLTELDGFTS--SNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
45-299 3.60e-47

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 171.48  E-value: 3.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  45 NVKFEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsn 123
Cdd:PTZ00454 141 DVTYSDIGGLDIQKQEIREAVeLPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAH---------HTTATF---- 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 124 dppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMER---RIVAQLL 200
Cdd:PTZ00454 208 --------------IRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELL 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 201 TCMDDLNNvaaTARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGF 280
Cdd:PTZ00454 274 NQMDGFDQ---TTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKI 350
                        250
                 ....*....|....*....
gi 341865579 281 VGADLMALCREAAMCAVNR 299
Cdd:PTZ00454 351 SAADIAAICQEAGMQAVRK 369
ftsH CHL00176
cell division protein; Validated
24-299 3.69e-47

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 176.39  E-value: 3.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  24 GEIEAVLQKKAKarglefqiSNVKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIA 103
Cdd:CHL00176 166 GKSKARFQMEAD--------TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 104 GaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPK 183
Cdd:CHL00176 238 G---------------------------EAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQ 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 184 R--EVASKDMER-RIVAQLLTCMDDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCR 260
Cdd:CHL00176 291 RgaGIGGGNDEReQTLNQLLTEMDGFK---GNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR 367
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 341865579 261 KLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMCAVNR 299
Cdd:CHL00176 368 NKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARR 406
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
387-646 5.28e-47

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 171.88  E-value: 5.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGAS---VRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDP 543
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 544 AILRPGRLDKTLFVGLPPPADRLAILKTITkngTKPPLDADVNLEAIAgdLRCDCYTGADLSALVREASICALRQEmarq 623
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHT---SKMTLAEDVDLEEFI--MAKDELSGADIKAICTEAGLLALRER---- 408
                        250       260
                 ....*....|....*....|...
gi 341865579 624 ksgnekgELKVSHKHFEEAFKKV 646
Cdd:PTZ00361 409 -------RMKVTQADFRKAKEKV 424
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
46-241 2.45e-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: 161.63  E-value: 2.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  46 VKFEDVGGNDMTLKEVCKMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndp 125
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAG--------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 126 pasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVA---SKDMERRIVAQLLTC 202
Cdd:cd19501   60 ------EAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggGHDEREQTLNQLLVE 133
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341865579 203 MDDLnnvAATARVLVIGATNRPDSLDPALRRAGRFDREI 241
Cdd:cd19501  134 MDGF---ESNTGVIVIAATNRPDVLDPALLRPGRFDRQV 169
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
48-241 8.03e-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: 160.20  E-value: 8.03e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  48 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndpp 126
Cdd:cd19502    2 YEDIGGLDEQIREIREVVeLPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVAN---------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 127 asasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDME-RRIVAQLLTCM 203
Cdd:cd19502   60 -----HTDATFIRVVGSELVQKYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQL 134
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 341865579 204 DDLNnvaATARVLVIGATNRPDSLDPALRRAGRFDREI 241
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 ...
68-241 2.24e-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: 156.12  E-value: 2.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  68 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 147
Cdd:cd19529   13 LLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE--------------SNAN-------------FISVKGPELLS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 148 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR-EVASKDMERRIVAQLLTCMDDLNNVAAtarVLVIGATNRPDS 226
Cdd:cd19529   66 KWVGESEKAIREIFRKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG---VVVIAATNRPDI 142
                        170
                 ....*....|....*
gi 341865579 227 LDPALRRAGRFDREI 241
Cdd:cd19529  143 IDPALLRAGRFDRLI 157
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
48-313 2.22e-43

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 161.86  E-value: 2.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  48 FEDVGGNDMTLKEVCKML-IHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsNDPP 126
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVeLPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVA-------------------NETS 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 127 ASasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 206
Cdd:PTZ00361 243 AT--------FLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQL 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 207 NNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLM 286
Cdd:PTZ00361 315 DGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIK 394
                        250       260
                 ....*....|....*....|....*...
gi 341865579 287 ALCREAAMCAVNRVLMKL-QEQQKKNPE 313
Cdd:PTZ00361 395 AICTEAGLLALRERRMKVtQADFRKAKE 422
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
393-556 5.31e-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: 5.31e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESG-----LNFISVKGPELLNMYV 467
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 468 GESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILR 547
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*....
gi 341865579 548 PGRLDKTLF 556
Cdd:cd19517  161 PGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
387-557 8.26e-43

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 151.94  E-value: 8.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNM 465
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 466 YVGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL-EARQQVFIMAATNRPDIIDPA 544
Cdd:cd19521   80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                        170
                 ....*....|...
gi 341865579 545 ILRpgRLDKTLFV 557
Cdd:cd19521  160 IRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
50-240 8.69e-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: 151.89  E-value: 8.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGND---MTLKEVckMLIHMRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAgAECSgmitahcsfdfsgsndpp 126
Cdd:cd19517    1 DIGGLShyiNQLKEM--VFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALA-AECS------------------ 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 127 aSASQELDLPILKVAapEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDL 206
Cdd:cd19517   60 -KGGQKVSFFMRKGA--DCLSKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGL 136
                        170       180       190
                 ....*....|....*....|....*....|....
gi 341865579 207 NNvaaTARVLVIGATNRPDSLDPALRRAGRFDRE 240
Cdd:cd19517  137 DN---RGQVVVIGATNRPDALDPALRRPGRFDRE 167
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
393-557 2.30e-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: 2.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALGLVT-PAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 471
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 472 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpg 549
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILR-- 158

                 ....*...
gi 341865579 550 RLDKTLFV 557
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 ...
70-241 2.35e-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: 2.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  70 HPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitaHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGV 149
Cdd:cd19528   15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIAN---------ECQANF------------------ISVKGPELLTMW 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 150 SGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKD---MERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDS 226
Cdd:cd19528   68 FGESEANVRDIFDKARAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMN---TKKNVFIIGATNRPDI 144
                        170
                 ....*....|....*
gi 341865579 227 LDPALRRAGRFDREI 241
Cdd:cd19528  145 IDPAILRPGRLDQLI 159
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
393-557 6.63e-40

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: 6.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKalGLVTP-AGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 471
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 472 RAVRQVFQRAKNSAPCVIFFDEVDALCPRR-SDRETGASVRVVNQLLTEMDGL-------EARQQVFIMAATNRPDIIDP 543
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 341865579 544 AILRpgRLDKTLFV 557
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 ...
68-239 3.41e-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: 139.16  E-value: 3.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  68 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahcsfdfSGSNdppasasqeldlpILKVAAPEIVS 147
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANE--------------SGAN-------------FISVKGPELLN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 148 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNnvaATARVLVIGATNRPDSL 227
Cdd:cd19530   69 KYVGESERAVRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE---ERSNVFVIAATNRPDII 145
                        170
                 ....*....|..
gi 341865579 228 DPALRRAGRFDR 239
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 ...
69-241 7.21e-37

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: 7.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  69 RHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGAecsgmitahCSFDFsgsndppasasqeldlpiLKVAAPEIVSG 148
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASE---------CGLNF------------------ISVKGPELLNK 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 149 VSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIGATNRPDSLD 228
Cdd:cd19526   67 YIGASEQNVRDLFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLD---GVEGLDGVYVLAATSRPDLID 143
                        170
                 ....*....|...
gi 341865579 229 PALRRAGRFDREI 241
Cdd:cd19526  144 PALLRPGRLDKLV 156
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
387-557 4.22e-36

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: 133.96  E-value: 4.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 387 PNVTWADIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMY 466
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGL-RGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 467 VGESERAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPA 544
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 341865579 545 ILRpgRLDKTLFV 557
Cdd:cd19525  176 ARR--RLVKRLYI 186
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
26-255 6.75e-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: 141.77  E-value: 6.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   26 IEAVLQKKAKARGLEfQISNVKFEDVGGNDMTLKevckmLIH------MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLA 99
Cdd:TIGR03689 160 FEAIPRTEVEDLVLE-EVPDVTYADIGGLGSQIE-----QIRdavelpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIA 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  100 HAIAGAECSGMitahcsfdFSGSNDPPAsasqeldlpILKVAAPEIVSGVSGESEQKLRELFEQAVSNA----PCIIFID 175
Cdd:TIGR03689 234 KAVANSLAARI--------GAEGGGKSY---------FLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFD 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  176 EIDAITPKREVA-SKDMERRIVAQLLTcmdDLNNVAATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERI 254
Cdd:TIGR03689 297 EMDSLFRTRGSGvSSDVETTVVPQLLA---EIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADI 373

                  .
gi 341865579  255 L 255
Cdd:TIGR03689 374 F 374
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
415-552 2.99e-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: 131.46  E-value: 2.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 415 PDQFKALGLVTPAGVLLAGPPGCGKTLLAKAV-----ANESGLnfisVKGPELLNMYVGESERAVRQVF------QRAK- 482
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFadaeeeQRRLg 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865579 483 -NSAPCVIFFDEVDALCPRRSDRETGASV--RVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLD 552
Cdd:cd19504  100 aNSGLHIIIFDEIDAICKQRGSMAGSTGVhdTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
cell_div_CdvC NF041006
cell division protein CdvC;
2-316 3.42e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 137.17  E-value: 3.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   2 KRKGKLKNKGSKRKKEDLQEVDGEIEAVLQKKAKarglefqisnVKFEDVGGndmtLKEVCKMLIH-----MRHPEVYHh 76
Cdd:NF041006  66 KRIEVLEELVPAEPAGPDVEKESDEELVVKEKPK----------VTFSDIVG----LEDVKEALKEaivypSKRPDLFP- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  77 LGVvpPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAAPEIVSGVSGESEQK 156
Cdd:NF041006 131 LGW--PRGILLYGPPGCGKTMLAAAVA---------------------------NEIDSEFIHVDAASIMSKWLGEAEKN 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 157 LRELFEQA-----VSNAPCIIFIDEIDAI--TPKREVASkdmERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLD- 228
Cdd:NF041006 182 VAKIFKKArekskEEGKPAIIFIDEIDALlgVYSSEVGG---EVRVRNQFLKEMDGLQDKSENYHVYVIGATNKPWRLDe 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 229 PALRragRFDREICLGIPDEASRERILQTLCRKLRLPQAFDFCHLAHLTPGFVGADLMALCREAAMcAVNRVLMKLQEQQ 308
Cdd:NF041006 259 PFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHM-RVVKEMFEKGLGE 334

                 ....*...
gi 341865579 309 KKNPEMED 316
Cdd:NF041006 335 PRPITMED 342
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
393-557 7.18e-35

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: 7.18e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKalGLVTPA-GVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESE 471
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 472 RAVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASVRVVNQLLTEMDGLEAR--QQVFIMAATNRPDIIDPAILRpg 549
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgdDRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 341865579 550 RLDKTLFV 557
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 ...
51-241 2.22e-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: 2.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  51 VGGNDmTLKEVCK--MLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppas 128
Cdd:cd19509    1 IAGLD-DAKEALKeaVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVA------------------------- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 129 asQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 208
Cdd:cd19509   54 --SESGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLN 131
                        170       180       190
                 ....*....|....*....|....*....|...
gi 341865579 209 vAATARVLVIGATNRPDSLDPALRRagRFDREI 241
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 ...
68-239 1.29e-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: 126.09  E-value: 1.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  68 MRHPEVYHhLGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVS 147
Cdd:cd19527   13 LEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIA---------TECSLNF------------------LSVKGPELIN 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 148 GVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKR--EVASKDMERRIVAQLLTCMDDLNNvaATARVLVIGATNRPD 225
Cdd:cd19527   65 MYIGESEANVREVFQKARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSS--SGQDVFVIGATNRPD 142
                        170
                 ....*....|....
gi 341865579 226 SLDPALRRAGRFDR 239
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 ...
393-557 3.59e-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: 3.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMailapvRNP---DQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGE 469
Cdd:cd19507    1 DVGGLDNLKDWLKK------RKAafsKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 470 SERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPDIIDPAILRP 548
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*....
gi 341865579 549 GRLDKTLFV 557
Cdd:cd19507  153 GRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
419-559 2.68e-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: 110.70  E-value: 2.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 419 KALGLVTPAGVLLAGPPGCGKTLLAKAVANES---GLNFISVKGPELLNMYVGESER---AVRQVFQRAKNSAPCVIFFD 492
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865579 493 EVDALCPRrsdretgASVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPGRLDKTLFVGL 559
Cdd:cd00009   92 EIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
45-241 3.24e-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: 111.11  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  45 NVKFEDVGGNDMTlKEVCK--MLIHMRHPEVYHHlGVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgs 122
Cdd:cd19521    3 NVKWEDVAGLEGA-KEALKeaVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVA------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 123 ndppasasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 202
Cdd:cd19521   62 --------TEANSTFFSVSSSDLVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQ 133
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341865579 203 MDDLNNvaATARVLVIGATNRPDSLDPALRRagRFDREI 241
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; ...
50-233 5.19e-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: 5.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGND---MTLKEvcKMLIHMRHPEVYHHLGVV-PPRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSFdfsgsndp 125
Cdd:cd19520    1 DIGGLDeviTELKE--LVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKE-------AGARF-------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 126 pasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDD 205
Cdd:cd19520   64 ------------INLQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDG 131
                        170       180
                 ....*....|....*....|....*...
gi 341865579 206 LNNvAATARVLVIGATNRPDSLDPALRR 233
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; ...
46-241 1.67e-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: 103.91  E-value: 1.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  46 VKFEDVGGNDM---TLKEVckMLIHMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgs 122
Cdd:cd19525   19 INWADIAGLEFakkTIKEI--VVWPMLRPDIFTGLRG-PPKGILLFGPPGTGKTLIGKCIA---------SQSGATF--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 123 ndppasasqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTC 202
Cdd:cd19525   84 ---------------FSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQ 148
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 341865579 203 MDDLnNVAATARVLVIGATNRPDSLDPALRRagRFDREI 241
Cdd:cd19525  149 LDGA-TTSSEDRILVVGATNRPQEIDEAARR--RLVKRL 184
ycf46 CHL00195
Ycf46; Provisional
332-570 1.99e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 107.41  E-value: 1.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 332 TSETQDELQRLLGLLrdQDPLSEEQM-------QGLCIE-----LNDFIVA-------LSSVQPSAKRE--------GFV 384
Cdd:CHL00195 144 ESEIKKELTRLIKSL--NIKIDSELLenltracQGLSLErirrvLSKIIATyktidenSIPLILEEKKQiisqteilEFY 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 385 TVpNVTWADIGALEDIREELTmailapvRNPDQF--KAL--GLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGP 460
Cdd:CHL00195 222 SV-NEKISDIGGLDNLKDWLK-------KRSTSFskQASnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 461 ELLNMYVGESERAVRQVFQRAKNSAPCVIFFDEVD-ALCPRRSDRETGASVRVVNQLLTEMDglEARQQVFIMAATNRPD 539
Cdd:CHL00195 294 KLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATANNID 371
                        250       260       270
                 ....*....|....*....|....*....|.
gi 341865579 540 IIDPAILRPGRLDKTLFVGLPPPADRLAILK 570
Cdd:CHL00195 372 LLPLEILRKGRFDEIFFLDLPSLEEREKIFK 402
ycf46 CHL00195
Ycf46; Provisional
39-285 3.85e-24

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 106.26  E-value: 3.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  39 LEFQISNVKFEDVGGNDmtlkeVCKMLIHMRH---PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahc 115
Cdd:CHL00195 218 LEFYSVNEKISDIGGLD-----NLKDWLKKRStsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIAN----------- 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 116 sfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERR 194
Cdd:CHL00195 282 ----------------DWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNR 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 195 IVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGRFDREICLGIPDEASRERILQTLCRKLRlP---QAFDFC 271
Cdd:CHL00195 346 VLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFR-PkswKKYDIK 419
                        250
                 ....*....|....
gi 341865579 272 HLAHLTPGFVGADL 285
Cdd:CHL00195 420 KLSKLSNKFSGAEI 433
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
81-244 2.12e-23

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: 96.83  E-value: 2.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  81 PPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasASQELDLPILKVAAPEIVSGVSGESEQK---L 157
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIAN------------------------ELFRPGAPFLYLNASDLLEGLVVAELFGhflV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 158 RELFEQAVSNAPCIIFIDEIDAITpkrevaskdmeRRIVAQLLTCMDDLNN-VAATARVLVIGATNRPDSLDPALRRAGR 236
Cdd:cd00009   74 RLLFELAEKAKPGVLFIDEIDSLS-----------RGAQNALLRVLETLNDlRIDRENVRVIGATNRPLLGDLDRALYDR 142

                 ....*...
gi 341865579 237 FDREICLG 244
Cdd:cd00009  143 LDIRIVIP 150
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
81-241 3.45e-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: 3.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  81 PPRGVLLHGPPGCGKTLLAHAIAgaecsgmitAHCSFDFsgsndppasasqeldlpiLKVAAPEIVSGVSGESEQKLREL 160
Cdd:cd19522   32 PWKGVLMVGPPGTGKTLLAKAVA---------TECGTTF------------------FNVSSSTLTSKYRGESEKLVRLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 161 FEQAVSNAPCIIFIDEIDAITPKREVASK-DMERRIVAQLLTCMDDLNNVAA----TARVLVIGATNRPDSLDPALRRag 235
Cdd:cd19522   85 FEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVGGASEnddpSKMVMVLAATNFPWDIDEALRR-- 162

                 ....*.
gi 341865579 236 RFDREI 241
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 ...
78-239 5.61e-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: 5.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  78 GVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAAPEIVSGVSGESEQKL 157
Cdd:cd19507   27 GLPTPKGLLLVGIQGTGKSLTAKAIAG---------------------------VWQLPLLRLDMGRLFGGLVGESESRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 158 RELFEQAVSNAPCIIFIDEID-AITPKREVASKDMERRIVAQLLTCMDDlnnvaATARVLVIGATNRPDSLDPALRRAGR 236
Cdd:cd19507   80 RQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQE-----KKKPVFVVATANNVQSLPPELLRKGR 154

                 ...
gi 341865579 237 FDR 239
Cdd:cd19507  155 FDE 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
50-241 1.59e-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: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGNDMTLKEVCKMLI-HMRHPEVYHHLGVvPPRGVLLHGPPGCGKTLLAHAIAgAECSGMItahcsfdfsgsndppas 128
Cdd:cd19524    1 DIAGQDLAKQALQEMVIlPSLRPELFTGLRA-PARGLLLFGPPGNGKTMLAKAVA-AESNATF----------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 129 asqeldlpiLKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVAQLLTCMDDLNN 208
Cdd:cd19524   62 ---------FNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQS 132
                        170       180       190
                 ....*....|....*....|....*....|...
gi 341865579 209 vAATARVLVIGATNRPDSLDPALRRagRFDREI 241
Cdd:cd19524  133 -NGDDRVLVMGATNRPQELDDAVLR--RFTKRV 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
71-241 1.96e-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: 94.86  E-value: 1.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  71 PEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIagaecSGMITAhcsfdfsgsNDPPAsasqeldlpilkVAAPEIVSGVS 150
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQI-----GKMLNA---------REPKI------------VNGPEILNKYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 151 GESEQKLRELFEQA---------VSNAPCIIFiDEIDAITPKREVASKD--MERRIVAQLLTCMD---DLNNVaatarvL 216
Cdd:cd19504   78 GESEANIRKLFADAeeeqrrlgaNSGLHIIIF-DEIDAICKQRGSMAGStgVHDTVVNQLLSKIDgveQLNNI------L 150
                        170       180
                 ....*....|....*....|....*
gi 341865579 217 VIGATNRPDSLDPALRRAGRFDREI 241
Cdd:cd19504  151 VIGMTNRKDLIDEALLRPGRLEVQM 175
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
393-557 3.89e-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: 90.71  E-value: 3.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 393 DIGALEDIREELTMAILAPVRNPDQFKALgLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGESER 472
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 473 AVRQVFQRAKNSAPCVIFFDEVDALCPRRSDRETGASvRVVNQLLTEMDGL--EARQQVFIMAATNRPDIIDPAILRpgR 550
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                 ....*..
gi 341865579 551 LDKTLFV 557
Cdd:cd19523  157 FSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
425-560 1.64e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 82.81  E-value: 1.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   425 TPAGVLLAGPPGCGKTLLAKAVANESGLNFISVK-----------------GPELLNMYVGESERAVRQVFQRAKNSAPC 487
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865579   488 VIFFDEVDALCPRRSDREtgasvRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPAILRPgRLDKTLFVGLP 560
Cdd:smart00382  81 VLILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
81-247 5.71e-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: 81.27  E-value: 5.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579    81 PPRGVLLHGPPGCGKTLLAHAIAG---AECSGMITAHCSFDFSGsndppasasqeldLPILKVAAPEIVSGVSGESEQKL 157
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARelgPPGGGVIYIDGEDILEE-------------VLDQLLLIIVGGKKASGSGELRL 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   158 RELFEQAVSNAPCIIFIDEIDAITpkrevaskDMERRIVAQLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRRAgRF 237
Cdd:smart00382  68 RLALALARKLKPDVLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RF 138
                          170
                   ....*....|
gi 341865579   238 DREICLGIPD 247
Cdd:smart00382 139 DRRIVLLLIL 148
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
50-233 2.30e-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: 71.07  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  50 DVGGNDM---TLKEvcKMLIHMRHPEVYHHLgVVPPRGVLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndpp 126
Cdd:cd19523    1 DIAGLGAlkaAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLA----------------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 127 asasQELDLPILKVAAPEIVSGVSGESEQKLRELFEQAVSNAPCIIFIDEIDAITPKReVASKDMERRIVAQLLTCMDDL 206
Cdd:cd19523   55 ----SQLGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDALLSSQ-DDEASPVGRLQVELLAQLDGV 129
                        170       180
                 ....*....|....*....|....*..
gi 341865579 207 NNvAATARVLVIGATNRPDSLDPALRR 233
Cdd:cd19523  130 LG-SGEDGVLVVCTTSKPEEIDESLRR 155
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
68-241 8.59e-14

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: 8.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  68 MRHPEVYHHLGVVPPRGVLLHGPPGCGKTLLAHAIAGaecsgmitahcsfdfsgsndppasasqELDLPILKVAapeiVS 147
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAG---------------------------ELDYDICDLN----LS 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 148 GVSGESEQKLRELfeqavSNAP--CIIFIDEIDA------ITPKREVASKDMERRIVAQLLTCMDdlnNVAATARVLVIG 219
Cdd:cd19510   58 EVVLTDDRLNHLL-----NTAPkqSIILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALD---GVASSEERIVFM 129
                        170       180
                 ....*....|....*....|..
gi 341865579 220 ATNRPDSLDPALRRAGRFDREI 241
Cdd:cd19510  130 TTNHIERLDPALIRPGRVDMKI 151
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
412-552 6.89e-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: 6.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 412 VRNPDQFKALGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFIsvkgpeLLNMY-VGESERAVRQVFQRAKNSApcVIF 490
Cdd:cd19510    9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNLSeVVLTDDRLNHLLNTAPKQS--IIL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 341865579 491 FDEVDALCPRRSDR-----ETGASVRV-VNQLLTEMDGL---EARqqVFIMaATNRPDIIDPAILRPGRLD 552
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 ...
429-544 7.86e-13

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 67.86  E-value: 7.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLN---------FISVKGPELLNMYVGESERAVRQVFQR------AKNSAPCVIFfDE 493
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVLI-DE 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 341865579 494 VDALCPRRSDRETGA----SVRVVNQLLTEMDGLEARQQVFIMAATNRPDIIDPA 544
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 ...
429-545 3.69e-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: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYvGESERAVRQVFQRAKNSAPCVIFF-DEVDALCPRRSDRETG 507
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEKIS 103
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 341865579 508 ASVR-VVNQLLTEMdGLEARQQVFIMaATNRPDIIDPAI 545
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 ...
268-307 1.95e-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: 53.31  E-value: 1.95e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 341865579  268 FDFCHLAHLTPGFVGADLMALCREAAMCAVNRVLMKLQEQ 307
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
421-553 5.00e-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: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 421 LGLVTPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLN--------------MYVGESERAVRQVFQRAKNSAP 486
Cdd:cd19505    7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYnkpdfgnddwidgmLILKESLHRLNLQFELAKAMSP 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341865579 487 CVIFFDEVDALCPRRSDRETGASVR-----VVNQLLTEMDGLEARQQVFImAATNRPDIIDPAILRPGRLDK 553
Cdd:cd19505   87 CIIWIPNIHELNVNRSTQNLEEDPKlllglLLNYLSRDFEKSSTRNILVI-ASTHIPQKVDPALIAPNRLDT 157
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
83-231 3.35e-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: 53.99  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  83 RGVLLHGPPGCGKTLLAHAIAGAecsgmITAHCSFDFSGSNdppasasqeldlpILKVAAPEIVSGVSGESEQKLRELF- 161
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQK-----LSIRLSSRYRYGQ-------------LIEINSHSLFSKWFSESGKLVTKMFq 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579 162 --EQAVSNAPCIIF--IDEIDAITPKREVASKDMER----RIVAQLLTCMDDLNNvaaTARVLVIGATNRPDSLDPAL 231
Cdd:cd19508  115 kiQELIDDKDALVFvlIDEVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKR---YHNNVILLTSNLLEKIDVAF 189
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
584-641 7.08e-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: 49.07  E-value: 7.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579  584 DVNLEAIAGdlRCDCYTGADLSALVREASICALRQEMArqksgnekgelKVSHKHFEE 641
Cdd:pfam17862   1 DVDLEELAE--RTEGFSGADLEALCREAALAALRRGLE-----------AVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
76-241 3.13e-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: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  76 HLGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMITAhcsfdfsgsndppaSASQELD-LPILKVAAPEIVSGVSGESE 154
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRI--------------SLNKLLYnKPDFGNDDWIDGMLILKESL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 155 QKLRELFEQAVSNAPCIIFIDEIDAITPKREVASKDMERRIVA-QLLTCMDDLNNVAATARVLVIGATNRPDSLDPALRR 233
Cdd:cd19505   72 HRLNLQFELAKAMSPCIIWIPNIHELNVNRSTQNLEEDPKLLLgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIA 151

                 ....*...
gi 341865579 234 AGRFDREI 241
Cdd:cd19505  152 PNRLDTCI 159
PRK04195 PRK04195
replication factor C large subunit; Provisional
429-595 4.47e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 53.00  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLnfisvkgpELLNMYVGESERA--VRQVFQRAKNSAPC------VIFFDEVDALCPr 500
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDYGW--------EVIELNASDQRTAdvIERVAGEAATSGSLfgarrkLILLDEVDGIHG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 501 RSDReTGAS--VRVVNqlltemdglEARQQVfIMAAtNrpDIIDPAiLRPGRlDKTLFVGLPPPADR--LAILKTITKN- 575
Cdd:PRK04195 113 NEDR-GGARaiLELIK---------KAKQPI-ILTA-N--DPYDPS-LRELR-NACLMIEFKRLSTRsiVPVLKRICRKe 176
                        170       180
                 ....*....|....*....|....
gi 341865579 576 GTKPPLDAdvnLEAIA----GDLR 595
Cdd:PRK04195 177 GIECDDEA---LKEIAersgGDLR 197
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
430-531 6.22e-07

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 52.54  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  430 LLAGPPGCGKTLLAKAVANE-SGL------NFISVKGPELLNMYVGESERAVRQVFQRAKNSapcVIFFDEVDALCPRRS 502
Cdd:TIGR03922 316 LFAGPPGTGKTTIARVVAKIyCGLgvlrkpLVREVSRADLIGQYIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGY 392
                          90       100
                  ....*....|....*....|....*....
gi 341865579  503 DRETGASVRVVNQLLTEMDGLEARQQVFI 531
Cdd:TIGR03922 393 GQKDPFGLEAIDTLLARMENDRDRLVVIG 421
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
429-499 6.89e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.01  E-value: 6.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFI-------SVKgpellnmyvgeserAVRQVFQRAKNSA----PCVIFFDEV--- 494
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDEIhrf 104
                         90
                 ....*....|
gi 341865579 495 -----DALCP 499
Cdd:PRK13342 105 nkaqqDALLP 114
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
429-499 1.32e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.21  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFISvkgpelLNmyvgeserAV-------RQVFQRAKNSA----PCVIFFDEV--- 494
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERRaygrRTILFVDEIhrf 117
                         90
                 ....*....|
gi 341865579 495 -----DALCP 499
Cdd:COG2256  118 nkaqqDALLP 127
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
85-177 1.69e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 50.85  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  85 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVsgeseQKLRELFEQA 164
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIA---------------------------GATDAPFEALSA--VTSGV-----KDLREVIEEA 84
                         90
                 ....*....|....*..
gi 341865579 165 VSNA----PCIIFIDEI 177
Cdd:PRK13342  85 RQRRsagrRTILFIDEI 101
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
429-591 2.49e-06

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: 49.78  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFISVKG-PELL-------NMYV-GESERAVRQ--VFQRaknsapcVIFFDEVDal 497
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpsdilgtYIYDqQTGEFEFRPgpLFAN-------VLLADEIN-- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 498 cprRSDRETGASvrvvnqLLTEMdgleARQQV-------------FIMAATNRPDIID-----PAILRpgRLDKTLFVGL 559
Cdd:COG0714  105 ---RAPPKTQSA------LLEAM----EERQVtipggtyklpepfLVIATQNPIEQEGtyplpEAQLD--RFLLKLYIGY 169
                        170       180       190
                 ....*....|....*....|....*....|..
gi 341865579 560 PPPADRLAILKTiTKNGTKPPLDADVNLEAIA 591
Cdd:COG0714  170 PDAEEEREILRR-HTGRHLAEVEPVLSPEELL 200
PRK04195 PRK04195
replication factor C large subunit; Provisional
47-104 2.71e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 50.30  E-value: 2.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579  47 KFEDVGGNDMTLKEVCKMLIHMRHPevyhhlgvVPPRGVLLHGPPGCGKTLLAHAIAG 104
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWIESWLKG--------KPKKALLLYGPPGVGKTSLAHALAN 61
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
85-177 4.82e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 49.28  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  85 VLLHGPPGCGKTLLAHAIAgaecsgmitahcsfdfsgsndppasasQELDLPILKVAApeIVSGVSgeseqKLRELFEQA 164
Cdd:COG2256   52 MILWGPPGTGKTTLARLIA---------------------------NATDAEFVALSA--VTSGVK-----DIREVIEEA 97
                         90
                 ....*....|....*..
gi 341865579 165 ----VSNAPCIIFIDEI 177
Cdd:COG2256   98 rerrAYGRRTILFVDEI 114
ycf2 CHL00206
Ycf2; Provisional
77-292 5.76e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.91  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   77 LGVVPPRGVLLHGPPGCGKTLLAHAIAGAECSGMIT--------------AHCSFDFSGSNDPPASASQELDLPILKVAA 142
Cdd:CHL00206 1625 LALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITvflnkfldnkpkgfLIDDIDIDDSDDIDDSDDIDRDLDTELLTM 1704
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  143 PEIVSG--VSGESEQKLRELFEQAVSNAPCIIFIDEIdaitpkREVASKDMERRIVAQLLTCMDDLNNVAATARVLVIGA 220
Cdd:CHL00206 1705 MNALTMdmMPKIDRFYITLQFELAKAMSPCIIWIPNI------HDLNVNESNYLSLGLLVNSLSRDCERCSTRNILVIAS 1778
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579  221 TNRPDSLDPALRRAGRFDREIC---LGIPdeaSRERILQTLCRKLRLPQAFDFCHL---AHLTPGFVGADLMALCREA 292
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 ...
429-462 1.16e-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: 45.95  E-value: 1.16e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 341865579  429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 462
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
428-547 1.70e-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: 44.98  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  428 GVLLAGPPGCGKTLLAK------------AVANESGLNFISVKGPelLNMYVGESERaVRQVFQRAKNSApCVIFFDEVD 495
Cdd:pfam07728   1 GVLLVGPPGTGKTELAErlaaalsnrpvfYVQLTRDTTEEDLFGR--RNIDPGGASW-VDGPLVRAAREG-EIAVLDEIN 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865579  496 alcprRSDRETgasVRVVNQLLTE-----MDGLE----ARQQVFIMAATNRPDI----IDPAILR 547
Cdd:pfam07728  77 -----RANPDV---LNSLLSLLDErrlllPDGGElvkaAPDGFRLIATMNPLDRglneLSPALRS 133
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
82-207 3.14e-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: 44.80  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   82 PRGVLLHGPPGCGKTLLAHAI---AGAECSGMITAHC--------------SFDFSGSNDPPASASQELDLPILKVAAPE 144
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCdenlpyspllealtREGLLRQLLDELESSLLEAWRAALLEALA 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 341865579  145 IVSGVSGESEQKLRELFEQAVSNA-----PCIIFIDEIDAItpkrevasKDMERRIVAQLLTCMDDLN 207
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLLDLLargerPLVLVLDDLQWA--------DEASLQLLAALLRLLESLP 163
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
429-462 3.93e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 46.28  E-value: 3.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 462
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
390-462 4.64e-05

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 45.75  E-value: 4.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865579  390 TWADIGALEDIREELTMAILAPVRNPDQfkalglvtPAGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPEL 462
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQLFIEAAKMRQEA--------LDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
428-481 8.88e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 44.99  E-value: 8.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865579  428 GVLLAGPPGCGKTLLAKAVANESG--LNFISVKGPELLNMYVGESErAVRQVFQRA 481
Cdd:pfam06068  52 AVLIAGPPGTGKTALAIAISKELGedTPFTSISGSEVYSLEMKKTE-ALTQAFRKA 106
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
85-293 1.21e-04

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: 44.39  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  85 VLLHGPPGCGKTLLAHAIAGAecsgmitAHCSF------------DFSGSNDPPASasqeldlpilkvaapeivsgvSGE 152
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARA-------LGLPFiriqftpdllpsDILGTYIYDQQ---------------------TGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 153 SEQKLRELFEQavsnapcIIFIDEIDAITPKREVAskdmerrivaqLLTCMD------DLNNVAATARVLVIGATNRPDS 226
Cdd:COG0714   86 FEFRPGPLFAN-------VLLADEINRAPPKTQSA-----------LLEAMEerqvtiPGGTYKLPEPFLVIATQNPIEQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341865579 227 -----LDPALRRagRFDREICLGIPDEASRERILqtlcrklrlpQAFDFCHLAHLTPGFVGADLMALCREAA 293
Cdd:COG0714  148 egtypLPEAQLD--RFLLKLYIGYPDAEEEREIL----------RRHTGRHLAEVEPVLSPEELLALQELVR 207
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
429-499 1.63e-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: 42.57  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  429 VLLAGPPGCGKTLLAKAVANESglnFISVKGPELLNM------------------YVGESERAvrQVFQRAKNSAPCVIF 490
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELL---FGDERALIRIDMseymeehsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVL 80

                  ....*....
gi 341865579  491 FDEVDALCP 499
Cdd:pfam07724  81 IDEIEKAHP 89
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
430-495 1.66e-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: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 430 LLAGPPGCGKTLLAKAVA---NESGLNFISVKGPELLNM------------YVGESERAvrQVFQRAKNSAPCVIFFDEV 494
Cdd:cd19499   45 LFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGG--QLTEAVRRKPYSVVLLDEI 122

                 .
gi 341865579 495 D 495
Cdd:cd19499  123 E 123
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
399-538 1.86e-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: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 399 DIREELTMAILAPVRNPDQFKALGLVTpaGVLLAGPPGCGKTLLAKAVANESGLNFISVKGPELLNMYVGES--ERAVRQ 476
Cdd:cd19506    1 DVRQLLTLYGILPLGSQAVHEKAPLVK--SLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 341865579 477 VFQRAKNSAPCVIFFDEVDALCPR---RSDRETGASvRVVNQLLTEMDGLEARQQVFIMAATNRP 538
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 ...
363-500 2.34e-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: 42.37  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 363 ELNDFIVAlssvQPSAKREGFVTVPNvTWADIGALEDIREEltmailapvrnpdqfkalglVTPAGVLLAGPPGCGKTLL 442
Cdd:cd19498    8 ELDKYIIG----QDEAKRAVAIALRN-RWRRMQLPEELRDE--------------------VTPKNILMIGPTGVGKTEI 62
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 341865579 443 AKAVANESGLNFISVKGPELLNM-YVGeseravRQVFQRAKNSAPCVIFFDEVDALCPR 500
Cdd:cd19498   63 ARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIAKR 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
428-475 2.68e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.81  E-value: 2.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 341865579 428 GVLLAGPPGCGKTLLAKAVANESGLN--FISVKGPELLNMYVGESE---RAVR 475
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALR 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
429-460 3.15e-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: 3.15e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 341865579 429 VLLAGPPGCGKTLLAKAVANESGLNFISVKGP 460
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
82-232 7.47e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.88  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  82 PRGVLLHGPPGCGKTLLAHAIAGAecsgmitAHCSfdfsgSNDPPASASQELDLPILKVAAPEivsgvsgeseqkLRELF 161
Cdd:COG0470   18 PHALLLHGPPGIGKTTLALALARD-------LLCE-----NPEGGKACGQCHSRLMAAGNHPD------------LLELN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 162 EQAVSNApciIFIDEIDAITPKREVASKDMERRIVaqLLTCMDDLNNVAATA----------RVLVIGATNRPDSLDPAL 231
Cdd:COG0470   74 PEEKSDQ---IGIDQIRELGEFLSLTPLEGGRKVV--IIDEADAMNEAAANAllktleeppkNTPFILIANDPSRLLPTI 148

                 .
gi 341865579 232 R 232
Cdd:COG0470  149 R 149
RecA cd00983
recombinase A; RecA is a bacterial enzyme which has roles in homologous recombination, DNA ...
82-185 1.40e-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: 40.62  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  82 PRG--VLLHGPPGCGKTLLA-HAIAGAECSGMItahCSF-DFSGSNDPPASASQELDLPILKVAAPEivsgvSGEseQKL 157
Cdd:cd00983   22 PRGriIEIYGPESSGKTTLAlHAIAEAQKLGGT---AAFiDAEHALDPEYAKKLGVDIDNLLVSQPD-----TGE--QAL 91
                         90       100
                 ....*....|....*....|....*....
gi 341865579 158 rELFEQAV-SNAPCIIFIDEIDAITPKRE 185
Cdd:cd00983   92 -EIADTLIrSGAVDLIVVDSVAALVPKAE 119
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
85-103 1.43e-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: 1.43e-03
                          10
                  ....*....|....*....
gi 341865579   85 VLLHGPPGCGKTLLAHAIA 103
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIA 54
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
82-178 1.46e-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: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579  82 PRGVLL-HGPPGCGKTLLAHAIAGAECSG---MITahcsFDFSgsndppaSASQELDLPILKVAAPEIVsgvsGESEQKL 157
Cdd:cd19499   40 PIGSFLfLGPTGVGKTELAKALAELLFGDednLIR----IDMS-------EYMEKHSVSRLIGAPPGYV----GYTEGGQ 104
                         90       100
                 ....*....|....*....|.
gi 341865579 158 reLFEQAVSNAPCIIFIDEID 178
Cdd:cd19499  105 --LTEAVRRKPYSVVLLDEIE 123
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
85-103 2.36e-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: 40.45  E-value: 2.36e-03
                         10
                 ....*....|....*....
gi 341865579  85 VLLHGPPGCGKTLLAHAIA 103
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIA 75
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
85-117 3.10e-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: 3.10e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 341865579   85 VLLHGPPGCGKTLLAHAIAGAECSGMITAHCSF 117
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALLKKLGLPKDSV 33
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
85-103 3.26e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 3.26e-03
                         10
                 ....*....|....*....
gi 341865579  85 VLLHGPPGCGKTLLAHAIA 103
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIA 72
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
430-497 4.52e-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: 4.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341865579 430 LLAGPPGCGKTLLAKAVANESGLNF--ISVKG----PEL---LNMYVGESERAVRQVFQRAKNSAPcVIFFDEVDAL 497
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFvrISLGGvrdeAEIrghRRTYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKI 116
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
85-182 5.03e-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: 38.33  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579   85 VLLHGPPGCGKTLLAHAIA---GAECSGMITAHCSfDFSGSNdppaSASQeldlpiLKVAAPEIVSgvSGESEQklreLF 161
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAellFGDERALIRIDMS-EYMEEH----SVSR------LIGAPPGYVG--YEEGGQ----LT 68
                          90       100
                  ....*....|....*....|.
gi 341865579  162 EQAVSNAPCIIFIDEIDAITP 182
Cdd:pfam07724  69 EAVRRKPYSIVLIDEIEKAHP 89
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
429-547 5.50e-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: 37.99  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341865579 429 VLLAGPPGCGKTLLAKAVANE----SGlnFISVKGPELLNMYVGESERAVRQVFQ------------RAKNSAPCVIFFD 492
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAGLlkptSG--EILIDGKDIAKLPLEELRRRIGYVPQlsggqrqrvalaRALLLNPDLLLLD 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341865579 493 EVD-ALcprrsDRETGASVRvvnQLLTEMdgleARQQVFIMAATNRPDIIDPAILR 547
Cdd:cd00267  106 EPTsGL-----DPASRERLL---ELLREL----AEEGRTVIIVTHDPELAELAADR 149
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
39-102 8.05e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 39.32  E-value: 8.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341865579  39 LEFQISNVK----FEDVGGNDMTLK---EVCKMLIHmrhpevYhhlgvvPPRG--VLLHGPPGCGKTLLAHAI 102
Cdd:COG1221   90 LAEKENNEEeedpFDNLIGANGSLKnaiEQAKAAIL------Y------PPKGlhTLILGPTGVGKSFFAELM 150
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
433-456 8.17e-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: 8.17e-03
                         10        20
                 ....*....|....*....|....
gi 341865579 433 GPPGCGKTLLAKAVANESGLNFIS 456
Cdd:cd02020    6 GPAGSGKSTVAKLLAKKLGLPYLD 29
 
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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