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Conserved domains on  [gi|31077102|ref|NP_852053|]
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mitochondrial inner membrane m-AAA protease component paraplegin isoform 1 [Rattus norvegicus]

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];
147-712 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 597.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465  70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465 139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465 217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFS-------------------------- 517
Cdd:COG0465 296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSgadlanlvneaallaarrnkkavtme 373
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 518 -----------GTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 585
Cdd:COG0465 374 dfeeaidrviaGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 586 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 660
Cdd:COG0465 453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|..
gi 31077102 661 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 712
Cdd:COG0465 532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-712 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 597.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465  70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465 139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465 217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFS-------------------------- 517
Cdd:COG0465 296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSgadlanlvneaallaarrnkkavtme 373
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 518 -----------GTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 585
Cdd:COG0465 374 dfeeaidrviaGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 586 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 660
Cdd:COG0465 453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|..
gi 31077102 661 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 712
Cdd:COG0465 532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-711 5.71e-180

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: 523.39  E-value: 5.71e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   504 FysQRLAELTPGFSGT-------------------------------------AKKSKILSKEEQRVVAFHESGHALVGW 546
Cdd:TIGR01241 249 L--KAVARRTPGFSGAdlanllneaallaarknkteitmndieeaidrviagpEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   547 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 625
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   626 KQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEV 700
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 31077102   701 INYEDIEALIG 711
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-710 6.05e-131

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 402.51  E-value: 6.05e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176 141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176 217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  423 GfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176 297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  503 SFysQRLAELTPGFSGT---------------AKKSKILSKE---------------------EQRVVAFHESGHALVGW 546
Cdd:CHL00176 376 SL--ELIARRTPGFSGAdlanllneaailtarRKKATITMKEidtaidrviaglegtpledskNKRLIAYHEVGHAIVGT 453
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  547 LLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAYS 623
Cdd:CHL00176 454 LLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLARQ 532
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  624 MVKQFGMApSIGPVSFPEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEK 698
Cdd:CHL00176 533 MVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQK 611
                        490
                 ....*....|..
gi 31077102  699 EVINYEDIEALI 710
Cdd:CHL00176 612 ETIDGDEFREIV 623
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-477 2.17e-101

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: 308.78  E-value: 2.17e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 31077102 466 MRPGRLDRHVFI 477
Cdd:cd19501 160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
524-709 1.31e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 257.91  E-value: 1.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   524 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 602
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   603 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLVGIG----RRPFSQGLQQMMDHEARLLVARAYRHTE 678
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 31077102   679 KVLLDNLDKLQALANALLEKEVINYEDIEAL 709
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
cell_div_CdvC NF041006
cell division protein CdvC;
306-519 5.98e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 136.79  E-value: 5.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGMGTAD---HVIVLASTN 456
Cdd:NF041006 177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLQDKSenyHVYVIGATN 251
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31077102  457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGT 519
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTAS 310
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
342-481 1.82e-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: 1.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102    342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31077102    405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 481
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
346-410 9.21e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 9.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102  346 LLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEViggLGAARV-RSLFKEAR--ARAPCIVyIDEI 410
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAA-----CRQGyrvrfttaADLVEQ---LAQARAdGRLGRLLRrlARYDLLI-IDEL 160
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-712 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 597.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465  70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465 139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465 217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFS-------------------------- 517
Cdd:COG0465 296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSgadlanlvneaallaarrnkkavtme 373
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 518 -----------GTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 585
Cdd:COG0465 374 dfeeaidrviaGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 586 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 660
Cdd:COG0465 453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|..
gi 31077102 661 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 712
Cdd:COG0465 532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-711 5.71e-180

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: 523.39  E-value: 5.71e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   504 FysQRLAELTPGFSGT-------------------------------------AKKSKILSKEEQRVVAFHESGHALVGW 546
Cdd:TIGR01241 249 L--KAVARRTPGFSGAdlanllneaallaarknkteitmndieeaidrviagpEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   547 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 625
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   626 KQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEV 700
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 31077102   701 INYEDIEALIG 711
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-710 6.05e-131

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 402.51  E-value: 6.05e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176 141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176 217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  423 GfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176 297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  503 SFysQRLAELTPGFSGT---------------AKKSKILSKE---------------------EQRVVAFHESGHALVGW 546
Cdd:CHL00176 376 SL--ELIARRTPGFSGAdlanllneaailtarRKKATITMKEidtaidrviaglegtpledskNKRLIAYHEVGHAIVGT 453
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  547 LLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAYS 623
Cdd:CHL00176 454 LLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLARQ 532
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  624 MVKQFGMApSIGPVSFPEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEK 698
Cdd:CHL00176 533 MVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQK 611
                        490
                 ....*....|..
gi 31077102  699 EVINYEDIEALI 710
Cdd:CHL00176 612 ETIDGDEFREIV 623
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
265-744 8.61e-112

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 352.80  E-value: 8.61e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  265 LAILWYVFRLAGMTGREG-GFSAFNQLKMARFTIVDGKTgkgvSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:PRK10733 111 LLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKT----TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPK 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:PRK10733 187 GVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGG 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSS 503
Cdd:PRK10733 267 -GHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLA--PD 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  504 FYSQRLAELTPGFS-------------------------------------GTAKKSKILSKEEQRVVAFHESGHALVGW 546
Cdd:PRK10733 344 IDAAIIARGTPGFSgadlanlvneaalfaargnkrvvsmvefekakdkimmGAERRSMVMTEAQKESTAYHEAGHAIIGR 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  547 LLEHTEAVMKVSIAPRtNAALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAYS 623
Cdd:PRK10733 424 LVPEHDPVHKVTIIPR-GRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIKVATNLARN 502
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  624 MVKQFGMAPSIGPVSFPEaQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEK 698
Cdd:PRK10733 503 MVTQWGFSEKLGPLLYAE-EEGEVFLGRsvakaKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKY 581
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 31077102  699 EVINYEDIEALIgppphGPKKMIAPQKWIDAEKEKQA--SGEEEAPAP 744
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 2.17e-101

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: 308.78  E-value: 2.17e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 31077102 466 MRPGRLDRHVFI 477
Cdd:cd19501 160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
524-709 1.31e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 257.91  E-value: 1.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   524 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 602
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   603 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLVGIG----RRPFSQGLQQMMDHEARLLVARAYRHTE 678
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 31077102   679 KVLLDNLDKLQALANALLEKEVINYEDIEAL 709
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
305-531 2.37e-81

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 262.25  E-value: 2.37e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG1222  74 DVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG1222 154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTS---GEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSG--------TAKKSKILSKEEQ 531
Cdd:COG1222 231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL--DKLAKLTEGFSGadlkaivtEAGMFAIREGRDT 304
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
305-518 1.56e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 225.10  E-value: 1.56e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 31077102  464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSG 518
Cdd:PRK03992 286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL--EELAELTEGASG 338
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 3.01e-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: 192.11  E-value: 3.01e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 396 EARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHV 475
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSS---GVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                ..
gi 31077102 476 FI 477
Cdd:cd19511 158 YV 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
308-518 4.00e-57

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: 199.75  E-value: 4.00e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 308 FQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFV-EVIGGL 385
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVsKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 386 gAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEeeqtLNQLLVEMDGMgtADHVIVLASTNRADVLDNAL 465
Cdd:COG0464 236 -EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRV----VNTLLTEMEEL--RSDVVVIAATNRPDLLDPAL 308
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 31077102 466 MRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSSFYSQRLAELTPGFSG 518
Cdd:COG0464 309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD--EDVDLEELAEATEGLSG 357
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
307-475 9.67e-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: 188.32  E-value: 9.67e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159
                       170
                ....*....|
gi 31077102 466 MRPGRLDRHV 475
Cdd:cd19502 160 LRPGRFDRKI 169
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
317-477 1.77e-54

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: 184.41  E-value: 1.77e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 317 AKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 397 ARARAPCIVYIDEIDAVGKKRSTSMsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDSSG---ESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 31077102 477 I 477
Cdd:cd19481 158 F 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-518 3.33e-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: 199.36  E-value: 3.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgFSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGAR---FDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31077102   465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSG 518
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL--EELAEMTEGYTG 658
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 6.04e-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: 177.70  E-value: 6.04e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 318 KLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 397 ARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARGGNIGD-AGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 31077102 477 I 477
Cdd:cd19528 161 I 161
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
310-477 3.34e-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: 170.16  E-value: 3.34e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRP 468
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREED----QREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 31077102 469 GRLDRHVFI 477
Cdd:cd19503 157 GRFDREVEI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
308-531 9.07e-49

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 171.99  E-value: 9.07e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 308 FQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMagpEFVEVIG---G 384
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTV---RLDSLIGsylG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 385 LGAARVRSLFKEARaRAPCIVYIDEIDAVGKKRS-TSMSGfsntEEEQTLNQLLVEMDGMgtADHVIVLASTNRADVLDN 463
Cdd:COG1223  78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGdQNDVG----EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDS 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102 464 ALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLtqPSSFYSQRLAELTPGFSG--------TAKKSKILSKEEQ 531
Cdd:COG1223 151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEGLSGadiekvlkTALKKAILEDREK 222
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
317-477 1.02e-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: 1.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 396 EARARAPCIVYIDEIDAVGKKR-STSMSGFSnteeEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRH 474
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVT----ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRL 156

                ...
gi 31077102 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 9.58e-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: 166.43  E-value: 9.58e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDYLKS-PERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILpPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMG----TADHVIVLASTNRADVLDNA 464
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESA----QREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                       170
                ....*....|.
gi 31077102 465 LMRPGRLDRHV 475
Cdd:cd19518 157 LRRAGRFDREI 167
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-518 1.20e-47

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: 180.49  E-value: 1.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEV----TGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 31077102   465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSG 518
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL--DKLAEVTHGFVG 382
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
306-490 1.67e-46

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 170.33  E-value: 1.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG-ADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180
                 ....*....|....*....|....*.
gi 31077102  465 LMRPGRLDRHVFIDLPTLQERREIFE 490
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQ 326
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 1.66e-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: 160.29  E-value: 1.66e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRP 468
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT----HGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                ....*....
gi 31077102 469 GRLDRHVFI 477
Cdd:cd19519 157 GRFDREIDI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
346-479 2.17e-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: 158.53  E-value: 2.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfs 425
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 31077102   426 ntEEEQTLNQLLVEMDGMGTADH-VIVLASTNRADVLDNALMrpGRLDRHVFIDL 479
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
307-492 2.21e-44

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 165.71  E-value: 2.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSG-GEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339
                        170       180
                 ....*....|....*....|....*..
gi 31077102  466 MRPGRLDRHVFIDLPTLQERREIFEQH 492
Cdd:PTZ00361 340 IRPGRIDRKIEFPNPDEKTKRRIFEIH 366
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
328-477 1.66e-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: 154.18  E-value: 1.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 328 LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19530  16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 408 DEIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFI 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 1.70e-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: 142.95  E-value: 1.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 329 KSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYID 408
Cdd:cd19526  14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31077102 409 EIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19526  94 EFDSIAPKRGHDSTGVT----DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
328-477 1.14e-36

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: 134.95  E-value: 1.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 328 LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19527  13 LEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31077102 408 DEIDAVGKKRSTsmSGFSNTEEEQTLNQLLVEMDGM-GTADHVIVLASTNRADVLDNALMRPGRLDRHVFI 477
Cdd:cd19527  92 DELDSLAPSRGN--SGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
306-494 1.86e-35

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.38  E-value: 1.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATE-AQVP---------FLAMA 374
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAARIgaegggksyFLNIK 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   375 GPEFVEVIGGLGAARVRSLFKEARARA----PCIVYIDEIDAVGKKRStsmSGFSNTEEEQTLNQLLVEMDGMGTADHVI 450
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRG---SGVSSDVETTVVPQLLAEIDGVESLDNVI 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31077102   451 VLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLK 494
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
cell_div_CdvC NF041006
cell division protein CdvC;
306-519 5.98e-35

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 136.79  E-value: 5.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006 100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGMGTAD---HVIVLASTN 456
Cdd:NF041006 177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLQDKSenyHVYVIGATN 251
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31077102  457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGT 519
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTAS 310
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
311-477 3.29e-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: 3.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 311 VAGMHEAKLEVREFVDY-LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAAR 389
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 390 VRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEeqtlNQLLVEMDGMGTA--DHVIVLASTNRADVLDNALMR 467
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR 155
                       170
                ....*....|
gi 31077102 468 pgRLDRHVFI 477
Cdd:cd19509 156 --RFEKRIYI 163
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
310-477 8.09e-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: 8.09e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLqlGAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfsnTEEEQTL---NQLLVEMDGMGTADH-------VIVLASTNR 457
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTS------EEHEASRrvkSELLVQMDGVGGASEnddpskmVMVLAATNF 152
                       170       180
                ....*....|....*....|
gi 31077102 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 6.08e-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: 110.66  E-value: 6.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 322 REFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVAT--EAQVPFLaMAGPEFVEVIGGLGAARVRSLFKEA-- 397
Cdd:cd19504  15 RAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKmlNAREPKI-VNGPEILNKYVGESEANIRKLFADAee 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 398 --RARAPC----IVYIDEIDAVGKKRStSMSGFSNTEEeQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRL 471
Cdd:cd19504  94 eqRRLGANsglhIIIFDEIDAICKQRG-SMAGSTGVHD-TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRL 171

                ....*.
gi 31077102 472 DRHVFI 477
Cdd:cd19504 172 EVQMEI 177
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 1.69e-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: 110.08  E-value: 1.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 303 GKGVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEV 381
Cdd:cd19525  16 GPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 382 IGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTA--DHVIVLASTNRAD 459
Cdd:cd19525  95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG----EHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQ 170
                       170
                ....*....|....*...
gi 31077102 460 VLDNALMRpgRLDRHVFI 477
Cdd:cd19525 171 EIDEAARR--RLVKRLYI 186
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
306-477 3.07e-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: 108.41  E-value: 3.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 306 VSFQDVAGMHEAKLEVREFVDYlksPERFLQL--GAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVI 382
Cdd:cd19521   4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 383 GGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGT-ADHVIVLASTNRADVL 461
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEAS----RRIKTELLVQMNGVGNdSQGVLVLGATNIPWQL 156
                       170
                ....*....|....*.
gi 31077102 462 DNALMRpgRLDRHVFI 477
Cdd:cd19521 157 DSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
310-473 8.08e-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: 107.21  E-value: 8.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEA-----QVPFLAMAGPEFVEVIG 383
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTeeeqTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS----IVSTLLALMDGLDNRGQVVVIGATNRPDALDP 156
                       170
                ....*....|
gi 31077102 464 ALMRPGRLDR 473
Cdd:cd19517 157 ALRRPGRFDR 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
310-477 1.32e-26

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 106.47  E-value: 1.32e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19524   1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGM--GTADHVIVLASTNRADVLDNALM 466
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEG----EHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                       170
                ....*....|.
gi 31077102 467 RpgRLDRHVFI 477
Cdd:cd19524 156 R--RFTKRVYV 164
ycf46 CHL00195
Ycf46; Provisional
338-538 3.87e-26

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 112.81  E-value: 3.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  338 GAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAM-AGPEFVEVIGGlGAARVRSLFKEARARAPCIVYIDEIDavgkk 416
Cdd:CHL00195 255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLFGGIVGE-SESRMRQMIRIAEALSPCILWIDEID----- 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  417 rstsmSGFSNTE---EEQTLNQLLvemdgmGT--------ADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQER 485
Cdd:CHL00195 329 -----KAFSNSEskgDSGTTNRVL------ATfitwlsekKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEER 397
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 31077102  486 REIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGTAKKSKILskeEQRVVAFHE 538
Cdd:CHL00195 398 EKIFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSII---EAMYIAFYE 447
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
310-467 8.12e-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: 104.43  E-value: 8.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLG-AKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTsmsgfsnTEEEQTL---NQLLVEMDGMGTADH--VIVLASTNRADVLD 462
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS-------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLD 153

                ....*
gi 31077102 463 NALMR 467
Cdd:cd19520 154 EAILR 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
312-479 2.95e-23

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 96.45  E-value: 2.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 312 AGMHEAKLEVREFVDYlksperflqlgaKVPKGALLLGPPGCGKTLLAKAVATEA---QVPFLAMAGPEFVE---VIGGL 385
Cdd:cd00009   1 VGQEEAIEALREALEL------------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEglvVAELF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKrstsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd00009  69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRG-----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                       170
                ....*....|....
gi 31077102 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 4.44e-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: 84.73  E-value: 4.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAK--LEVREfVDYLKSPERFlqlGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19507   1 DVGGLDNLKdwLKKRK-AAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 388 ARVRSLFKEARARAPCIVYIDEID-AVGKKRSTSMSGFSNteeeQTLNQLLVEMDGMGTAdhVIVLASTNRADVLDNALM 466
Cdd:cd19507  77 SRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSS----RVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELL 150
                       170
                ....*....|.
gi 31077102 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 3.30e-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: 3.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 321 VREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfveviGGLGAARVRSLFKEARAR 400
Cdd:cd19510   2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31077102 401 ApcIVYIDEIDA--VGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFI 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 1.42e-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: 77.62  E-value: 1.42e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLgAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEqtlnqLLVEMDGMGTA--DHVIVLASTNRADVLDNALM 466
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154

                .
gi 31077102 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 1.82e-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: 1.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102    342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31077102    405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 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 1.11e-10

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 60.85  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 335 LQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMA-------GPEFVEVIGGLGAA-------RVRSLFKEARAR 400
Cdd:cd19505   5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynKPDFGNDDWIDGMLilkeslhRLNLQFELAKAM 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31077102 401 APCIVYIDEIDAVGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDR 473
Cdd:cd19505  85 SPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
346-465 1.29e-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: 57.15  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfVEVIGGLGAARVRSLFKEA-RARAPCIVYIDEIDAVGKKRSTS-MSg 423
Cdd:cd19512  26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEkIS- 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 31077102 424 fsnTEEEQTLNQLLVEMdGMGTADHVIVLAStNRADVLDNAL 465
Cdd:cd19512 104 ---EDLRAALNAFLYRT-GEQSNKFMLVLAS-NQPEQFDWAI 140
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
346-416 1.78e-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: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA---RARAPC-IVYIDEI 410
Cdd:COG1219 113 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydVEKAERgIIYIDEI 183

                ....*.
gi 31077102 411 DAVGKK 416
Cdd:COG1219 184 DKIARK 189
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
346-416 4.03e-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: 51.83  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 346 LLLGPPGCGKTLLAKAVATEAQVPF-------LAMAG--PEFVEVIgglgaarVRSLFKEAR---ARAP-CIVYIDEIDA 412
Cdd:cd19497  54 LLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAGyvGEDVENI-------LLKLLQAADydvERAQrGIVYIDEIDK 126

                ....
gi 31077102 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 4.14e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.60  E-value: 4.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102   346 LLLGPPGCGKTLLAKAVAtEA--QVPFLAMAGPEFVEV--------IGGLGAARVRSLFKEArARAPCIVYIDEID 411
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTEedlfgrrnIDPGGASWVDGPLVRA-AREGEIAVLDEIN 76
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
346-416 8.49e-07

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 52.08  E-value: 8.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA-----RA-RApcIVYID 408
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydveKAqRG--IVYID 180

                 ....*...
gi 31077102  409 EIDAVGKK 416
Cdd:PRK05342 181 EIDKIARK 188
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
341-420 2.32e-06

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: 48.53  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 341 VPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVigGLGAARVRSLFKEArarAPCIVYIDEIDAVGKKRSTS 420
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEV--GYVGRDVESIIRDL---VEGIVFIDEIDKIAKRGGSS 119
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
346-410 4.01e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 4.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31077102  346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
PRK04195 PRK04195
replication factor C large subunit; Provisional
307-411 5.72e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.53  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102  307 SFQDVAGMHEAKLEVREFVdylkspERFLQlgaKVPKGALLL-GPPGCGKTLLAKAVATEaqvpflamAGPEFVE----- 380
Cdd:PRK04195  12 TLSDVVGNEKAKEQLREWI------ESWLK---GKPKKALLLyGPPGVGKTSLAHALAND--------YGWEVIElnasd 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 31077102  381 ---------VIGglGAARVRSLFKEARArapcIVYIDEID 411
Cdd:PRK04195  75 qrtadvierVAG--EAATSGSLFGARRK----LILLDEVD 108
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
145-242 6.89e-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: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   145 LFIIAIVMSLLNSLSTSGGS----ISWADFVNeMLAKGEVQRVQVVPESDVVEVYLHPGAVVfGRPRLAlMYRMQVANID 220
Cdd:pfam06480   5 LLILLVLLLLFLLFLLSSSSstkeISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKD-GSKFTT-YFIPSLPNVD 81
                          90       100
                  ....*....|....*....|..
gi 31077102   221 KFEEKLRAAEDELNIESKDRIP 242
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVKPP 103
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
346-410 7.00e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 49.28  E-value: 7.00e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31077102 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:COG2256  53 ILWGPPGTGKTTLARLIANATDAEFVALSA-----VTSGV--KDIREVIEEARERRaygrRTILFVDEI 114
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
343-378 2.02e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.02e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 31077102 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 7.41e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.00  E-value: 7.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 310 DVAGMHEAKLEVREFVDYLKsperflqLGAKVpKGALLL--GPPGCGKTLLAKAVATeaqvpflAMaGPEFVEV-IGGL- 385
Cdd:cd19500  11 DHYGLEDVKERILEYLAVRK-------LKGSM-KGPILClvGPPGVGKTSLGKSIAR-------AL-GRKFVRIsLGGVr 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 31077102 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 7.93e-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: 7.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 31077102   343 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 378
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
313-441 1.94e-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: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102   313 GMHEAKLEVREFVDYLKSPERFLQLGAKVPKGA---LLLGPPGCGKTLLAKAVATeaqvpFLAMAG----PEFVEV---- 381
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAK-----IYCGLGvlrkPLVREVsrad 354
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31077102   382 -IG---GLGAARVRSLFKEARARapcIVYIDEIDAVGKKRSTSMSGFSNteeeQTLNQLLVEMD 441
Cdd:TIGR03922 355 lIGqyiGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGL----EAIDTLLARME 411
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
346-463 3.38e-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: 38.25  E-value: 3.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31077102 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIgglgAARVRSLFKEARaraPCIVYIDEIdavgkkrSTSMSGFS 425
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTI----LEAIEDLIEEKK---LDIIIIDSL-------SSLARASQ 67
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 31077102 426 NTEEEQTLNQLLVEMDGMGTAdHVIVLASTNRADVLDN 463
Cdd:cd01120  68 GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDID 104
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
343-410 3.79e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 3.79e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31077102 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 4.66e-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: 38.25  E-value: 4.66e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 31077102   346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGP 376
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGP 67
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
308-364 8.13e-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: 8.13e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102 308 FQDVAGMHEAK--LEVrefvdylksperflqlgakvpkgA-------LLLGPPGCGKTLLAKAVAT 364
Cdd:COG0606 191 LADVKGQEQAKraLEI-----------------------AaagghnlLMIGPPGSGKTMLARRLPG 233
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
346-410 9.21e-03

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 38.61  E-value: 9.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31077102  346 LLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEViggLGAARV-RSLFKEAR--ARAPCIVyIDEI 410
Cdd:NF038214  94 LLLGPPGTGKTHLAIALGYAA-----CRQGyrvrfttaADLVEQ---LAQARAdGRLGRLLRrlARYDLLI-IDEL 160
 
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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