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Conserved domains on  [gi|148539988|ref|NP_694816|]
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mitochondrial inner membrane m-AAA protease component paraplegin isoform 1 preproprotein [Mus musculus]

Protein Classification

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein( domain architecture ID 11422021)

ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein such as ATP-dependent zinc metalloprotease FtsH, which targets both cytoplasmic and membrane proteins and plays a role in quality control of integral membrane proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-749 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 147 IIALVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465   70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465  139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDN 463
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465  296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465  374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQE----GLMGIGRRPFSQGLQQM 698
Cdd:COG0465  453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflGRDIGQSRNYSEETARE 532
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148539988 699 MDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-749 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 147 IIALVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465   70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465  139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDN 463
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465  296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465  374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQE----GLMGIGRRPFSQGLQQM 698
Cdd:COG0465  453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflGRDIGQSRNYSEETARE 532
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148539988 699 MDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-748 0e+00

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: 589.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  424 fSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  504 FysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:TIGR01241 249 L--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  584 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 662
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  663 KQFGMAPSIGPVSFpEAQEGLMGIGR-----RPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEV 737
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 148539988  738 INYEDIEALIG 748
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-747 4.89e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 450.27  E-value: 4.89e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176 141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176 217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 423 GfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176 297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 503 SFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKeEQRVVAFHESGHALVG 582
Cdd:CHL00176 376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 583 WLLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAY 659
Cdd:CHL00176 453 TLLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLAR 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 660 SMVKQFGMApSIGPVSFPEAQEGLMGIGR-----RPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLE 734
Cdd:CHL00176 532 QMVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQ 610
                        490
                 ....*....|...
gi 148539988 735 KEVINYEDIEALI 747
Cdd:CHL00176 611 KETIDGDEFREIV 623
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-477 9.96e-102

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: 310.70  E-value: 9.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNAL 465
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 148539988 466 MRPGRLDRHVFI 477
Cdd:cd19501  160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
561-746 1.13e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 259.07  E-value: 1.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  561 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 639
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  640 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQE---GLMGIG-RRPFSQGLQQMMDHEAKLLVAKAYRHTE 715
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGnvfLGRGMGkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 148539988  716 KVLLDNLDKLQALANALLEKEVINYEDIEAL 746
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
cell_div_CdvC NF041006
cell division protein CdvC;
306-535 2.90e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.50  E-value: 2.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGM---GTTDHVIVLASTN 456
Cdd:NF041006 177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLqdkSENYHVYVIGATN 251
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
342-481 1.81e-14

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: 71.25  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988   342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539988   405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 481
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-749 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 147 IIALVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465    1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465   70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465  139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDN 463
Cdd:COG0465  217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465  296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465  374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQE----GLMGIGRRPFSQGLQQM 698
Cdd:COG0465  453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESEGevflGRDIGQSRNYSEETARE 532
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148539988 699 MDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465  533 IDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-748 0e+00

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: 589.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  424 fSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  504 FysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:TIGR01241 249 L--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  584 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 662
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  663 KQFGMAPSIGPVSFpEAQEGLMGIGR-----RPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEV 737
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 148539988  738 INYEDIEALIG 748
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-747 4.89e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 450.27  E-value: 4.89e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176 141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176 217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 423 GfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176 297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 503 SFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKeEQRVVAFHESGHALVG 582
Cdd:CHL00176 376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 583 WLLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAY 659
Cdd:CHL00176 453 TLLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLAR 531
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 660 SMVKQFGMApSIGPVSFPEAQEGLMGIGR-----RPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLE 734
Cdd:CHL00176 532 QMVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQ 610
                        490
                 ....*....|...
gi 148539988 735 KEVINYEDIEALI 747
Cdd:CHL00176 611 KETIDGDEFREIV 623
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
265-781 1.06e-130

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 403.26  E-value: 1.06e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 265 LAILWYVFRLAGMTGREG-GFSAFNQLKMARFTIVDGKTgkgvSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:PRK10733 111 LLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKT----TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPK 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:PRK10733 187 GVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGG 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 424 fSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSS 503
Cdd:PRK10733 267 -GHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLA--PD 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 504 FYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:PRK10733 344 IDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGR 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 584 LLEHTEAVMKVSIAPRtNAALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAYS 660
Cdd:PRK10733 424 LVPEHDPVHKVTIIPR-GRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIKVATNLARN 502
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 661 MVKQFGMAPSIGPVSFPEaQEGLMGIGR-----RPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEK 735
Cdd:PRK10733 503 MVTQWGFSEKLGPLLYAE-EEGEVFLGRsvakaKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKY 581
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 148539988 736 EVINYEDIEALIgppphGPKKMIAPQKWIDAEKERQA--SGEEEAPAP 781
Cdd:PRK10733 582 ETIDAPQIDDLM-----ARRDVRPPAGWEEPGASNNSddNGTPKAPRP 624
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-477 9.96e-102

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: 310.70  E-value: 9.96e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNAL 465
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 148539988 466 MRPGRLDRHVFI 477
Cdd:cd19501  160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
305-559 1.29e-95

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 300.77  E-value: 1.29e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDN 463
Cdd:COG1222  154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTS---GEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG1222  231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL--DKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTME 308
                        250
                 ....*....|....*.
gi 148539988 544 NFEYAVERVIAGTAKK 559
Cdd:COG1222  309 DLEKAIEKVKKKTETA 324
Peptidase_M41 pfam01434
Peptidase family M41;
561-746 1.13e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 259.07  E-value: 1.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  561 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 639
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  640 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQE---GLMGIG-RRPFSQGLQQMMDHEAKLLVAKAYRHTE 715
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGnvfLGRGMGkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 148539988  716 KVLLDNLDKLQALANALLEKEVINYEDIEAL 746
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
305-561 1.82e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 262.85  E-value: 1.82e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDN 463
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL--EELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                        250
                 ....*....|....*...
gi 148539988 544 NFEYAVERVIAGTAKKSK 561
Cdd:PRK03992 364 DFLKAIEKVMGKEEKDSM 381
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
308-552 2.95e-69

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: 233.26  E-value: 2.95e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 308 FQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFV-EVIGGL 385
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVsKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 gAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEeeqtLNQLLVEMDGMgtTDHVIVLASTNRADVLDNAL 465
Cdd:COG0464  236 -EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRV----VNTLLTEMEEL--RSDVVVIAATNRPDLLDPAL 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 466 MRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNF 545
Cdd:COG0464  309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD--EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                 ....*..
gi 148539988 546 EYAVERV 552
Cdd:COG0464  385 LEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-540 4.16e-62

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: 222.47  E-value: 4.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGAR---FDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539988  465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSV 540
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL--EELAEMTEGYTGADIEAVCREAAMAALRESIGSP 680
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
317-477 4.75e-57

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: 191.73  E-value: 4.75e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19511    1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 396 EARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHV 475
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSS---GVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                 ..
gi 148539988 476 FI 477
Cdd:cd19511  158 YV 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
307-475 2.72e-56

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: 190.24  E-value: 2.72e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNAL 465
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159
                        170
                 ....*....|
gi 148539988 466 MRPGRLDRHV 475
Cdd:cd19502  160 LRPGRFDRKI 169
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
308-551 4.03e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 192.79  E-value: 4.03e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 308 FQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMagpEFVEVIG---G 384
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTV---RLDSLIGsylG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 385 LGAARVRSLFKEARaRAPCIVYIDEIDAVGKKRS-TSMSGfsntEEEQTLNQLLVEMDGMgtTDHVIVLASTNRADVLDN 463
Cdd:COG1223   78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGdQNDVG----EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 464 ALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLtqPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG1223  151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKE 226

                 ....*...
gi 148539988 544 NFEYAVER 551
Cdd:COG1223  227 DLEEALKQ 234
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
317-477 6.54e-55

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 185.95  E-value: 6.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 317 AKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 397 ARARAPCIVYIDEIDAVGKKRSTSMsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19481   81 ARRLAPCILFIDEIDAIGRKRDSSG---ESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 148539988 477 I 477
Cdd:cd19481  158 F 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
306-553 2.64e-54

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 192.67  E-value: 2.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNA 464
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG-ADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSF--YSQRLAELtpgfSGADIANICNEAALHAAREGHTSVHT 542
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLedFVSRPEKI----SAADIAAICQEAGMQAVRKNRYVILP 376
                        250
                 ....*....|.
gi 148539988 543 FNFEYAVERVI 553
Cdd:PTZ00454 377 KDFEKGYKTVV 387
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-534 7.26e-54

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: 198.98  E-value: 7.26e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEV----TGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAR 534
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL--DKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
318-477 6.30e-52

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: 178.09  E-value: 6.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 318 KLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19528    2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 397 ARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19528   82 ARAAAPCVLFFDELDSIAKARGGNIGD-AGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 148539988 477 I 477
Cdd:cd19528  161 I 161
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
307-553 1.45e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 183.43  E-value: 1.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNAL 465
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSG-GEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 466 MRPGRLDRHVFIDLPTLQERREIFEQHLKglKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNF 545
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTS--KMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                 ....*...
gi 148539988 546 EYAVERVI 553
Cdd:PTZ00361 418 RKAKEKVL 425
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
310-477 2.17e-49

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: 170.94  E-value: 2.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19503    1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRP 468
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED----QREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                 ....*....
gi 148539988 469 GRLDRHVFI 477
Cdd:cd19503  157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
317-477 1.38e-48

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


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 168.83  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19529    1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 396 EARARAPCIVYIDEIDAVGKKR-STSMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRH 474
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVT----ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRL 156

                 ...
gi 148539988 475 VFI 477
Cdd:cd19529  157 IYI 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
310-475 8.94e-48

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: 166.81  E-value: 8.94e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDYLKS-PERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILpPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMG----TTDHVIVLASTNRADVLDNA 464
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESA----QREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                        170
                 ....*....|.
gi 148539988 465 LMRPGRLDRHV 475
Cdd:cd19518  157 LRRAGRFDREI 167
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
310-477 1.05e-45

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: 161.06  E-value: 1.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19519    1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRP 468
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT----HGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                 ....*....
gi 148539988 469 GRLDRHVFI 477
Cdd:cd19519  157 GRFDREIDI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
346-479 1.81e-45

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: 158.91  E-value: 1.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfs 425
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 148539988  426 ntEEEQTLNQLLVEMDGM-GTTDHVIVLASTNRADVLDNALMrpGRLDRHVFIDL 479
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
328-477 1.38e-43

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 154.95  E-value: 1.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 328 LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19530   16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 408 DEIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFI 477
Cdd:cd19530   96 DEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
329-476 1.01e-39

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: 143.72  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 329 KSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYID 408
Cdd:cd19526   14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148539988 409 EIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19526   94 EFDSIAPKRGHDSTGVT----DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
cell_div_CdvC NF041006
cell division protein CdvC;
306-535 2.90e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.50  E-value: 2.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGM---GTTDHVIVLASTN 456
Cdd:NF041006 177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLqdkSENYHVYVIGATN 251
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
328-477 7.50e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 135.72  E-value: 7.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 328 LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19527   13 LEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148539988 408 DEIDAVGKKRSTsmSGFSNTEEEQTLNQLLVEMDGM-GTTDHVIVLASTNRADVLDNALMRPGRLDRHVFI 477
Cdd:cd19527   92 DELDSLAPSRGN--SGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
306-494 4.69e-35

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 140.23  E-value: 4.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATE-AQVP---------FLAMA 374
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAARIgaegggksyFLNIK 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  375 GPEFVEVIGGLGAARVRSLFKEARARA----PCIVYIDEIDAVGKKRStsmSGFSNTEEEQTLNQLLVEMDGMGTTDHVI 450
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRG---SGVSSDVETTVVPQLLAEIDGVESLDNVI 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 148539988  451 VLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLK 494
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
311-477 3.79e-34

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 128.24  E-value: 3.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 311 VAGMHEAKLEVREFVDY-LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAAR 389
Cdd:cd19509    1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 390 VRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEeqtlNQLLVEMDGMGTT--DHVIVLASTNRADVLDNALMR 467
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR 155
                        170
                 ....*....|
gi 148539988 468 pgRLDRHVFI 477
Cdd:cd19509  156 --RFEKRIYI 163
ycf46 CHL00195
Ycf46; Provisional
338-535 3.66e-29

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 122.05  E-value: 3.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 338 GAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAM-AGPEFVEVIGGlGAARVRSLFKEARARAPCIVYIDEIDavgkk 416
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLFGGIVGE-SESRMRQMIRIAEALSPCILWIDEID----- 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 417 rstsmSGFSNTE---EEQTLNQLLvemdgmGT--------TDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQER 485
Cdd:CHL00195 329 -----KAFSNSEskgDSGTTNRVL------ATfitwlsekKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEER 397
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 148539988 486 REIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:CHL00195 398 EKIFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYE 447
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
310-477 8.52e-29

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: 113.16  E-value: 8.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLqlGAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfsnTEEEQTL---NQLLVEMDGMGTTDH-------VIVLASTNR 457
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTS------EEHEASRrvkSELLVQMDGVGGASEnddpskmVMVLAATNF 152
                        170       180
                 ....*....|....*....|
gi 148539988 458 ADVLDNALMRpgRLDRHVFI 477
Cdd:cd19522  153 PWDIDEALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
322-477 4.43e-28

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: 111.43  E-value: 4.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 322 REFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVAT--EAQVPFLaMAGPEFVEVIGGLGAARVRSLFKEA-- 397
Cdd:cd19504   15 RAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKmlNAREPKI-VNGPEILNKYVGESEANIRKLFADAee 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 398 --RARAPC----IVYIDEIDAVGKKRStSMSGFSNTEEeQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRL 471
Cdd:cd19504   94 eqRRLGANsglhIIIFDEIDAICKQRG-SMAGSTGVHD-TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRL 171

                 ....*.
gi 148539988 472 DRHVFI 477
Cdd:cd19504  172 EVQMEI 177
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
306-477 1.00e-27

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: 109.95  E-value: 1.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 306 VSFQDVAGMHEAKLEVREFVDYlksPERFLQL--GAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVI 382
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 383 GGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGT-TDHVIVLASTNRADVL 461
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEAS----RRIKTELLVQMNGVGNdSQGVLVLGATNIPWQL 156
                        170
                 ....*....|....*.
gi 148539988 462 DNALMRpgRLDRHVFI 477
Cdd:cd19521  157 DSAIRR--RFEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
303-477 2.26e-27

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: 109.69  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 303 GKGVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEV 381
Cdd:cd19525   16 GPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 382 IGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTT--DHVIVLASTNRAD 459
Cdd:cd19525   95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG----EHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQ 170
                        170
                 ....*....|....*...
gi 148539988 460 VLDNALMRpgRLDRHVFI 477
Cdd:cd19525  171 EIDEAARR--RLVKRLYI 186
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
310-473 4.03e-27

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: 108.37  E-value: 4.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEA-----QVPFLAMAGPEFVEVIG 383
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTsmsgfsntEEEQT----LNQLLVEMDGMGTTDHVIVLASTNRAD 459
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSS--------KQEQIhasiVSTLLALMDGLDNRGQVVVIGATNRPD 152
                        170
                 ....*....|....
gi 148539988 460 VLDNALMRPGRLDR 473
Cdd:cd19517  153 ALDPALRRPGRFDR 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
310-477 1.00e-26

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 106.86  E-value: 1.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19524    1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGM--GTTDHVIVLASTNRADVLDNALM 466
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEG----EHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 148539988 467 RpgRLDRHVFI 477
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
310-467 5.90e-26

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: 104.81  E-value: 5.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLG-AKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19520    1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTsmsgfsnTEEEQTL---NQLLVEMDGMGTTDH--VIVLASTNRADVLD 462
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS-------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLD 153

                 ....*
gi 148539988 463 NALMR 467
Cdd:cd19520  154 EAILR 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
312-479 1.41e-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: 97.60  E-value: 1.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 312 AGMHEAKLEVREFVDYlksperflqlgaKVPKGALLLGPPGCGKTLLAKAVATEA---QVPFLAMAGPEFVE---VIGGL 385
Cdd:cd00009    1 VGQEEAIEALREALEL------------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEglvVAELF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKrstsmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNAL 465
Cdd:cd00009   69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRG-----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                        170
                 ....*....|....
gi 148539988 466 MRPGRLDRHVFIDL 479
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
310-477 1.26e-19

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: 86.65  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAK--LEVREfVDYLKSPERFlqlGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19507    1 DVGGLDNLKdwLKKRK-AAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 388 ARVRSLFKEARARAPCIVYIDEID-AVGKKRSTSMSGFSNteeeQTLNQLLVEMDgmGTTDHVIVLASTNRADVLDNALM 466
Cdd:cd19507   77 SRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSS----RVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELL 150
                        170
                 ....*....|.
gi 148539988 467 RPGRLDRHVFI 477
Cdd:cd19507  151 RKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
321-477 3.26e-17

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: 79.32  E-value: 3.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 321 VREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfveviGGLGAARVRSLFKEARAR 400
Cdd:cd19510    2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 401 ApcIVYIDEIDA--VGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFI 477
Cdd:cd19510   77 S--IILLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
310-467 2.07e-16

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: 77.23  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLgAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEqtlnqLLVEMDGMGTT--DHVIVLASTNRADVLDNALM 466
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154

                 .
gi 148539988 467 R 467
Cdd:cd19523  155 R 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
342-481 1.81e-14

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: 71.25  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988   342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148539988   405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 481
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
335-473 1.25e-11

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: 63.55  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 335 LQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMA-------GPEFVEVIGGLGAA-------RVRSLFKEARAR 400
Cdd:cd19505    5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynKPDFGNDDWIDGMLilkeslhRLNLQFELAKAM 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148539988 401 APCIVYIDEIDAVGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDR 473
Cdd:cd19505   85 SPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
507-546 3.67e-11

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: 58.32  E-value: 3.67e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 148539988  507 QRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFE 546
Cdd:pfam17862   5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
346-465 1.20e-09

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: 57.54  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfVEVIGGLGAARVRSLFKEA-RARAPCIVYIDEIDAVGKKRSTS-MSg 423
Cdd:cd19512   26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEkIS- 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 148539988 424 fsnTEEEQTLNQLLVEMdGMGTTDHVIVLAStNRADVLDNAL 465
Cdd:cd19512  104 ---EDLRAALNAFLYRT-GEQSNKFMLVLAS-NQPEQFDWAI 140
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
346-416 1.85e-07

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 54.28  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA---RARAPC-IVYIDEI 410
Cdd:COG1219  113 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydVEKAERgIIYIDEI 183

                 ....*.
gi 148539988 411 DAVGKK 416
Cdd:COG1219  184 DKIARK 189
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
341-454 2.73e-07

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: 51.23  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 341 VPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVigGLGAARVRSLFKEArarAPCIVYIDEIDAVGKKRSTS 420
Cdd:cd19498   45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEV--GYVGRDVESIIRDL---VEGIVFIDEIDKIAKRGGSS 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148539988 421 MSGFSNTEEEQTLNQlLVEMD------GMGTTDHVIVLAS 454
Cdd:cd19498  120 GPDVSREGVQRDLLP-IVEGStvstkyGPVKTDHILFIAA 158
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
346-416 3.87e-07

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 52.22  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPF-------LAMAG--PEFVEVIgglgaarVRSLFKEAR---ARAP-CIVYIDEIDA 412
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAGyvGEDVENI-------LLKLLQAADydvERAQrGIVYIDEIDK 126

                 ....
gi 148539988 413 VGKK 416
Cdd:cd19497  127 IARK 130
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
346-411 3.96e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.98  E-value: 3.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539988  346 LLLGPPGCGKTLLAKAVAtEA--QVPFLAMAGPEFVEV--------IGGLGAARVRSLFKEArARAPCIVYIDEID 411
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTEedlfgrrnIDPGGASWVDGPLVRA-AREGEIAVLDEIN 76
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
346-416 8.90e-07

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 52.08  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA-----RA-RApcIVYID 408
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydveKAqRG--IVYID 180

                 ....*...
gi 148539988 409 EIDAVGKK 416
Cdd:PRK05342 181 EIDKIARK 188
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
346-410 4.71e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 4.71e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
PRK04195 PRK04195
replication factor C large subunit; Provisional
307-411 5.79e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.53  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 307 SFQDVAGMHEAKLEVREFVdylkspERFLQlgaKVPKGALLL-GPPGCGKTLLAKAVATEaqvpflamAGPEFVE----- 380
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI------ESWLK---GKPKKALLLyGPPGVGKTSLAHALAND--------YGWEVIElnasd 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 148539988 381 ---------VIGglGAARVRSLFKEARArapcIVYIDEID 411
Cdd:PRK04195  75 qrtadvierVAG--EAATSGSLFGARRK----LILLDEVD 108
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
346-410 8.35e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.90  E-value: 8.35e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDAEFVALSA-----VTSGV--KDIREVIEEARERRaygrRTILFVDEI 114
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
145-242 8.56e-06

FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only membrane-bound ATP-dependent protease universally conserved in prokaryotes. It only efficiently degrades proteins that have a low thermodynamic stability - e.g. it lacks robust unfoldase activity. This feature may be key and implies that this could be a criterion for degrading a protein. In Oenococcus oeni FtsH is involved in protection against environmental stress, and shows increased expression under heat or osmotic stress. These two lines of evidence suggest that it is a fundamental prokaryotic self-protection mechanism that checks if proteins are correctly folded (personal obs: Yeats C). The precise function of this N-terminal region is unclear.


Pssm-ID: 377663 [Multi-domain]  Cd Length: 103  Bit Score: 45.29  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  145 LFIIALVMSLLNSLSTSGGSISWADFVNeMLAKGEVQRVQVVPESDVVEVYLHPGAVVfGRPRLAlMYRMQVANIDKFEE 224
Cdd:pfam06480   9 LVLLLLFLLFLLSSSSSTKEISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKD-GSKFTT-YFIPSLPNVDSLLE 85
                          90
                  ....*....|....*...
gi 148539988  225 KLRAAEDELNIESKDRIP 242
Cdd:pfam06480  86 KLEDALEEKGVKVSVKPP 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
343-378 2.04e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.04e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 148539988 343 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 378
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
310-415 6.62e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.39  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 310 DVAGMHEAKLEVREFVDYLKsperflqLGAKVpKGALLL--GPPGCGKTLLAKAVATeaqvpflAMaGPEFVEV-IGGL- 385
Cdd:cd19500   11 DHYGLEDVKERILEYLAVRK-------LKGSM-KGPILClvGPPGVGKTSLGKSIAR-------AL-GRKFVRIsLGGVr 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 148539988 386 -------------GA--ARVRSLFKEARARAPCIVyIDEIDAVGK 415
Cdd:cd19500   75 deaeirghrrtyvGAmpGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
343-378 8.27e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 42.30  E-value: 8.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148539988  343 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 378
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
346-554 1.36e-03

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: 41.31  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPF-------------------LAMAGPEFVEVIGGLGAArvrslfkeararapcIVY 406
Cdd:COG0714   35 LLEGVPGVGKTTLAKALARALGLPFiriqftpdllpsdilgtyiYDQQTGEFEFRPGPLFAN---------------VLL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 407 IDEIDavgkkRSTsmsgfsnteeEQTLNQLLVEMDGM-----GTT----DHVIVLASTNRADV-----LDNALmrpgrLD 472
Cdd:COG0714  100 ADEIN-----RAP----------PKTQSALLEAMEERqvtipGGTyklpEPFLVIATQNPIEQegtypLPEAQ-----LD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 473 R---HVFIDLPTLQERREIFEQHLKGlkltqpssfysqRLAELTPGFSGADIAnicneAALHAAREGHtsVHTFNFEYAV 549
Cdd:COG0714  160 RfllKLYIGYPDAEEEREILRRHTGR------------HLAEVEPVLSPEELL-----ALQELVRQVH--VSEAVLDYIV 220

                 ....*
gi 148539988 550 ERVIA 554
Cdd:COG0714  221 DLVRA 225
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
346-463 2.12e-03

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 38.64  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIgglgAARVRSLFKEARaraPCIVYIDEIdavgkkrSTSMSGFS 425
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTI----LEAIEDLIEEKK---LDIIIIDSL-------SSLARASQ 67
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 148539988 426 NTEEEQTLNQLLVEMDGMGTTdHVIVLASTNRADVLDN 463
Cdd:cd01120   68 GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDID 104
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
313-460 2.19e-03

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: 41.37  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  313 GMHEAKLEVREFVDYLKSPERFLQLGAKVPKGA---LLLGPPGCGKTLLAKAVATeaqvpFLAMAG----PEFVEV---- 381
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAK-----IYCGLGvlrkPLVREVsrad 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148539988  382 -IG---GLGAARVRSLFKEARARapcIVYIDEIDAVGKKRSTSMSGFSNteeeQTLNQLLVEMDgmGTTDHVIVLASTNR 457
Cdd:TIGR03922 355 lIGqyiGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGL----EAIDTLLARME--NDRDRLVVIGAGYR 425

                  ...
gi 148539988  458 ADV 460
Cdd:TIGR03922 426 KDL 428
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
343-410 4.09e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 4.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148539988 343 KGALLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEvigGLGAARV-RSLFKEAR--ARAPCIVyIDEI 410
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEA-----CRAGyrvrfttaPDLVN---ELKEARAdGRLERLLKrlAKVDLLI-LDEL 169
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
346-376 4.74e-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: 38.64  E-value: 4.74e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 148539988  346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGP 376
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGP 67
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
308-364 8.93e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.25  E-value: 8.93e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148539988 308 FQDVAGMHEAK--LEVrefvdylksperflqlgakvpkgA-------LLLGPPGCGKTLLAKAVAT 364
Cdd:COG0606  191 LADVKGQEQAKraLEI-----------------------AaagghnlLMIGPPGSGKTMLARRLPG 233
 
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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