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Conserved domains on  [gi|2172663947|ref|NP_001386039|]
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mitochondrial inner membrane m-AAA protease component paraplegin isoform 2 [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];
147-749 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465    70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465   139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465   217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465   296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465   374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 697
Cdd:COG0465   453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2172663947 698 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-749 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465    70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465   139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465   217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465   296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465   374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 697
Cdd:COG0465   453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2172663947 698 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-748 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 590.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 504 FysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:TIGR01241 249 L--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 584 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 662
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 663 KQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEV 737
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 2172663947 738 INYEDIEALIG 748
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-747 2.98e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 451.04  E-value: 2.98e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176  141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 423 GfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176  297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 503 SFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKeEQRVVAFHESGHALVG 582
Cdd:CHL00176  376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 583 WLLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAY 659
Cdd:CHL00176  453 TLLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLAR 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 660 SMVKQFGMApSIGPVSFPEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLE 734
Cdd:CHL00176  532 QMVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQ 610
                         490
                  ....*....|...
gi 2172663947 735 KEVINYEDIEALI 747
Cdd:CHL00176  611 KETIDGDEFREIV 623
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-477 4.03e-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: 309.16  E-value: 4.03e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                         170
                  ....*....|..
gi 2172663947 466 MRPGRLDRHVFI 477
Cdd:cd19501   160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
561-746 3.34e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 257.53  E-value: 3.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 561 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 639
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 640 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLVGIG----RRPFSQGLQQMMDHEARLLVARAYRHTE 715
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2172663947 716 KVLLDNLDKLQALANALLEKEVINYEDIEAL 746
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
cell_div_CdvC NF041006
cell division protein CdvC;
306-535 3.72e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.11  E-value: 3.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGMGTAD---HVIVLASTN 456
Cdd:NF041006  177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLQDKSenyHVYVIGATN 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:NF041006  252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
342-481 1.85e-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: 1.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947  342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172663947  405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 481
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
147-749 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 675.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 147 IIAIVMSLLNSLSTSGGS---ISWADFVnEMLAKGEVQRVQVVPesDVVEVYLHPGAvvfgrprlALMYRMQVANIDKFE 223
Cdd:COG0465     1 IALLLVLLFNLFSSSSSSvkeISYSEFL-QLVEAGKVKSVTIQG--DRITGTLKDGT--------KTRFTTYRVNDPELV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 224 EKLRAAEDELNIESKDRipvsykrTGFFGNALYALGMTAVGLAILWYVFRlaGMTGREGGFSAFNQLKmARFtIVDGKTG 303
Cdd:COG0465    70 DLLEEKGVEVTAKPPEE-------SSWLLSLLISLLPILLLIGLWIFFMR--RMQGGGGGAMSFGKSK-AKL-YDEDKPK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 304 kgVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG0465   139 --VTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG0465   217 GVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG-GHDEREQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG0465   296 ALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 544 NFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTnAALGFSQMLP-RDQYLFTKEQL 622
Cdd:COG0465   374 DFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG-RALGYTMQLPeEDRYLYTKEEL 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 623 FERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQ 697
Cdd:COG0465   453 LDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAY-GESEGEVFLGRdigqsRNYSEETAR 531
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2172663947 698 MMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGP 749
Cdd:COG0465   532 EIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
265-748 0e+00

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 590.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 265 LAILWYVFRLAgMTGreGGFSAFNQLKM-ARFTIvdgKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:TIGR01241  16 LVGVWFFFRRQ-MQG--GGGRAFSFGKSkAKLLN---EEKPKVTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIPK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:TIGR01241  90 GVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSS 503
Cdd:TIGR01241 170 -GNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 504 FysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:TIGR01241 249 L--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 584 LLEHTEAVMKVSIAPRTNaALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMV 662
Cdd:TIGR01241 327 LLKDADPVHKVTIIPRGQ-ALGYTQFLPEeDKYLYTKSQLLAQIAVLLGGRAAEEIIFGEVTTGASNDIKQATNIARAMV 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 663 KQFGMAPSIGPVSFpEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEKEV 737
Cdd:TIGR01241 406 TEWGMSDKLGPVAY-GSDGGDVFLGRgfakaKEYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKET 484
                         490
                  ....*....|.
gi 2172663947 738 INYEDIEALIG 748
Cdd:TIGR01241 485 ITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
265-747 2.98e-149

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 451.04  E-value: 2.98e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 265 LAILWYVFRLAGMTGREGGFSAFNQLKM-ARF-TIVDgktgKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVP 342
Cdd:CHL00176  141 IGVLWFFFQRSSNFKGGPGQNLMNFGKSkARFqMEAD----TGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIP 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 343 KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMS 422
Cdd:CHL00176  217 KGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIG 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 423 GfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPS 502
Cdd:CHL00176  297 G-GNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDV 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 503 SFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKeEQRVVAFHESGHALVG 582
Cdd:CHL00176  376 SL--ELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSK-NKRLIAYHEVGHAIVG 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 583 WLLEHTEAVMKVSIAPRTNaALGFSQMLP-RDQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAY 659
Cdd:CHL00176  453 TLLPNHDPVQKVTLIPRGQ-AKGLTWFTPeEDQSLVSRSQILARIVGALGGRAAEEVVFgsTEVTTGASNDLQQVTNLAR 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 660 SMVKQFGMApSIGPVSFPEAQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLE 734
Cdd:CHL00176  532 QMVTRFGMS-SIGPISLESNNSTDPFLGRfmqrnSEYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQ 610
                         490
                  ....*....|...
gi 2172663947 735 KEVINYEDIEALI 747
Cdd:CHL00176  611 KETIDGDEFREIV 623
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
265-781 2.46e-131

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 404.80  E-value: 2.46e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 265 LAILWYVFRLAGMTGREG-GFSAFNQLKMARFTIVDGKTgkgvSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPK 343
Cdd:PRK10733  111 LLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQIKT----TFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPK 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 344 GALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSG 423
Cdd:PRK10733  187 GVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGG 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 424 fSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSS 503
Cdd:PRK10733  267 -GHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLA--PD 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 504 FYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGW 583
Cdd:PRK10733  344 IDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAYHEAGHAIIGR 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 584 LLEHTEAVMKVSIAPRtNAALGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAISF--SRVTSGAQDDLRKVTRIAYS 660
Cdd:PRK10733  424 LVPEHDPVHKVTIIPR-GRALGVTFFLPEgDAISASRQKLESQISTLYGGRLAEEIIYgpEHVSTGASNDIKVATNLARN 502
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 661 MVKQFGMAPSIGPVSFPEaQEGLVGIGR-----RPFSQGLQQMMDHEARLLVARAYRHTEKVLLDNLDKLQALANALLEK 735
Cdd:PRK10733  503 MVTQWGFSEKLGPLLYAE-EEGEVFLGRsvakaKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILHAMKDALMKY 581
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 2172663947 736 EVINYEDIEALIgppphGPKKMIAPQKWIDAEKEKQA--SGEEEAPAP 781
Cdd:PRK10733  582 ETIDAPQIDDLM-----ARRDVRPPAGWEEPGASNNSddNGTPKAPRP 624
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
306-477 4.03e-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: 309.16  E-value: 4.03e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19501     1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19501    81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGG-GHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                         170
                  ....*....|..
gi 2172663947 466 MRPGRLDRHVFI 477
Cdd:cd19501   160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
305-559 2.62e-95

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 300.00  E-value: 2.62e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:COG1222    74 DVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYI 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:COG1222   154 GEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTS---GEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDP 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG1222   231 ALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL--DKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTME 308
                         250
                  ....*....|....*.
gi 2172663947 544 NFEYAVERVIAGTAKK 559
Cdd:COG1222   309 DLEKAIEKVKKKTETA 324
Peptidase_M41 pfam01434
Peptidase family M41;
561-746 3.34e-81

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 257.53  E-value: 3.34e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 561 KILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAaLGFSQMLPR-DQYLFTKEQLFERMCMALGGRAAEAIS 639
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEeDKLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 640 FSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLVGIG----RRPFSQGLQQMMDHEARLLVARAYRHTE 715
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVFLGRgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2172663947 716 KVLLDNLDKLQALANALLEKEVINYEDIEAL 746
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
305-561 1.98e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 262.85  E-value: 1.98e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 305 GVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIG 383
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:PRK03992  207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGD-REVQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDP 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:PRK03992  286 AILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL--EELAELTEGASGADLKAICTEAGMFAIRDDRTEVTME 363
                         250
                  ....*....|....*...
gi 2172663947 544 NFEYAVERVIAGTAKKSK 561
Cdd:PRK03992  364 DFLKAIEKVMGKEEKDSM 381
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
308-552 1.21e-68

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 231.72  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 308 FQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFV-EVIGGL 385
Cdd:COG0464   156 LDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVsKYVGET 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 gAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEeeqtLNQLLVEMDGMgtADHVIVLASTNRADVLDNAL 465
Cdd:COG0464   236 -EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRV----VNTLLTEMEEL--RSDVVVIAATNRPDLLDPAL 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 466 MRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTqpSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNF 545
Cdd:COG0464   309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD--EDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDL 384

                  ....*..
gi 2172663947 546 EYAVERV 552
Cdd:COG0464   385 LEALERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-540 6.68e-62

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 221.70  E-value: 6.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgFSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGAR---FDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172663947 465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAREGHTSV 540
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL--EELAEMTEGYTGADIEAVCREAAMAALRESIGSP 680
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
317-477 2.63e-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: 192.50  E-value: 2.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19511     1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 396 EARARAPCIVYIDEIDAVGKKRSTSMSGfsnTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHV 475
Cdd:cd19511    81 KARQAAPCIIFFDEIDSLAPRRGQSDSS---GVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                  ..
gi 2172663947 476 FI 477
Cdd:cd19511   158 YV 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
308-551 4.60e-56

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 192.41  E-value: 4.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 308 FQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMagpEFVEVIG---G 384
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTV---RLDSLIGsylG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARaRAPCIVYIDEIDAVGKKRS-TSMSGfsntEEEQTLNQLLVEMDGMgtADHVIVLASTNRADVLDN 463
Cdd:COG1223    78 ETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGdQNDVG----EVKRVVNALLQELDGL--PSGSVVIAATNHPELLDS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 464 ALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLtqPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTF 543
Cdd:COG1223   151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKE 226

                  ....*...
gi 2172663947 544 NFEYAVER 551
Cdd:COG1223   227 DLEEALKQ 234
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
307-475 1.02e-55

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: 188.70  E-value: 1.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:cd19502     1 TYEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd19502    81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPAL 159
                         170
                  ....*....|
gi 2172663947 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 1.82e-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: 184.79  E-value: 1.82e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 317 AKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 397 ARARAPCIVYIDEIDAVGKKRSTSMsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19481    81 ARRLAPCILFIDEIDAIGRKRDSSG---ESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                  .
gi 2172663947 477 I 477
Cdd:cd19481   158 F 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
306-534 1.01e-53

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 198.59  E-value: 1.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:TIGR01243 175 VTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:TIGR01243 255 ESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEV----TGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPA 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAAR 534
Cdd:TIGR01243 331 LRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL--DKLAEVTHGFVGADLAALAKEAAMAALR 398
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
306-553 2.20e-53

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 189.97  E-value: 2.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:PTZ00454  142 VTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNA 464
Cdd:PTZ00454  222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTG-ADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 465 LMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSF--YSQRLAELtpgfSGADIANICNEAALHAAREGHTSVHT 542
Cdd:PTZ00454  301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLedFVSRPEKI----SAADIAAICQEAGMQAVRKNRYVILP 376
                         250
                  ....*....|.
gi 2172663947 543 FNFEYAVERVI 553
Cdd:PTZ00454  377 KDFEKGYKTVV 387
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 5.70e-52

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 178.09  E-value: 5.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 318 KLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKE 396
Cdd:cd19528     2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 397 ARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19528    82 ARAAAPCVLFFDELDSIAKARGGNIGD-AGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                  .
gi 2172663947 477 I 477
Cdd:cd19528   161 I 161
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
307-553 1.50e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 183.43  E-value: 1.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 307 SFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGL 385
Cdd:PTZ00361  181 SYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:PTZ00361  261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSG-GEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPAL 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 466 MRPGRLDRHVFIDLPTLQERREIFEQHLKglKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNF 545
Cdd:PTZ00361  340 IRPGRIDRKIEFPNPDEKTKRRIFEIHTS--KMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADF 417

                  ....*...
gi 2172663947 546 EYAVERVI 553
Cdd:PTZ00361  418 RKAKEKVL 425
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
310-477 3.41e-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: 170.55  E-value: 3.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19503     1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRP 468
Cdd:cd19503    81 NLREIFEEARSHAPSIIFIDEIDALAPKREED----QREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                  ....*....
gi 2172663947 469 GRLDRHVFI 477
Cdd:cd19503   157 GRFDREVEI 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
317-477 8.65e-49

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: 169.21  E-value: 8.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 317 AKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFK 395
Cdd:cd19529     1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 396 EARARAPCIVYIDEIDAVGKKR-STSMSGFSnteeEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRH 474
Cdd:cd19529    81 KARQVAPCVIFFDEIDSIAPRRgTTGDSGVT----ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRL 156

                  ...
gi 2172663947 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 9.68e-48

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 166.81  E-value: 9.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDYLKS-PERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19518     1 DIGGMDSTLKELCELLIHPILpPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMG----TADHVIVLASTNRADVLDNA 464
Cdd:cd19518    81 KIRELFDQAISNAPCIVFIDEIDAITPKRESA----QREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                         170
                  ....*....|.
gi 2172663947 465 LMRPGRLDRHV 475
Cdd:cd19518   157 LRRAGRFDREI 167
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
310-477 1.41e-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: 160.68  E-value: 1.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19519     1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRP 468
Cdd:cd19519    81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKT----HGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                  ....*....
gi 2172663947 469 GRLDRHVFI 477
Cdd:cd19519   157 GRFDREIDI 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
346-479 2.21e-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: 2.21e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGfs 425
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2172663947 426 ntEEEQTLNQLLVEMDGMGTADH-VIVLASTNRADVLDNALMrpGRLDRHVFIDL 479
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
328-477 1.66e-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: 154.57  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 328 LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 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 1.21e-39

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 143.72  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 329 KSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYID 408
Cdd:cd19526    14 KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFD 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2172663947 409 EIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRLDRHVF 476
Cdd:cd19526    94 EFDSIAPKRGHDSTGVT----DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
cell_div_CdvC NF041006
cell division protein CdvC;
306-535 3.72e-39

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 149.11  E-value: 3.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFlQLGAkvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGG 384
Cdd:NF041006  100 VTFSDIVGLEDVKEALKEAIVYpSKRPDLF-PLGW--PRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 385 LGAARVRSLFKEARARA-----PCIVYIDEIDAVGKKRSTSMSGfsnteEEQTLNQLLVEMDGMGTAD---HVIVLASTN 456
Cdd:NF041006  177 EAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEVGG-----EVRVRNQFLKEMDGLQDKSenyHVYVIGATN 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 457 RADVLDNALMRpgRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFysQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:NF041006  252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDL--DELAEMTEGYTASDIRDIVQAAHMRVVKE 326
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
328-477 6.48e-37

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 136.10  E-value: 6.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 328 LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYI 407
Cdd:cd19527    13 LEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARDAKPCVIFF 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2172663947 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 2.40e-35

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 141.00  E-value: 2.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATE-AQVP---------FLAMA 374
Cdd:TIGR03689 179 VTYADIGGLGSQIEQIRDAVELpFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAARIgaegggksyFLNIK 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 375 GPEFVEVIGGLGAARVRSLFKEARARA----PCIVYIDEIDAVGKKRStsmSGFSNTEEEQTLNQLLVEMDGMGTADHVI 450
Cdd:TIGR03689 259 GPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRG---SGVSSDVETTVVPQLLAEIDGVESLDNVI 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2172663947 451 VLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLK 494
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLT 379
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
311-477 2.50e-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: 128.62  E-value: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 311 VAGMHEAKLEVREFVDY-LKSPERFlQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAAR 389
Cdd:cd19509     1 IAGLDDAKEALKEAVILpSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 390 VRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEeqtlNQLLVEMDGMGTA--DHVIVLASTNRADVLDNALMR 467
Cdd:cd19509    80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVK----TEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR 155
                         170
                  ....*....|
gi 2172663947 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 7.02e-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: 113.54  E-value: 7.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLqlGAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19522     1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfsnTEEEQTL---NQLLVEMDGMGTADH-------VIVLASTNR 457
Cdd:cd19522    79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTS------EEHEASRrvkSELLVQMDGVGGASEnddpskmVMVLAATNF 152
                         170       180
                  ....*....|....*....|
gi 2172663947 458 ADVLDNALMRpgRLDRHVFI 477
Cdd:cd19522   153 PWDIDEALRR--RLEKRIYI 170
ycf46 CHL00195
Ycf46; Provisional
338-535 2.10e-28

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 119.74  E-value: 2.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 338 GAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAM-AGPEFVEVIGGlGAARVRSLFKEARARAPCIVYIDEIDavgkk 416
Cdd:CHL00195  255 GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLdVGKLFGGIVGE-SESRMRQMIRIAEALSPCILWIDEID----- 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 417 rstsmSGFSNTE---EEQTLNQLLvemdgmGT--------ADHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQER 485
Cdd:CHL00195  329 -----KAFSNSEskgDSGTTNRVL------ATfitwlsekKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEER 397
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2172663947 486 REIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAARE 535
Cdd:CHL00195  398 EKIFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIAFYE 447
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
322-477 4.88e-28

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 111.04  E-value: 4.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 322 REFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVAT--EAQVPFLaMAGPEFVEVIGGLGAARVRSLFKEA-- 397
Cdd:cd19504    15 RAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKmlNAREPKI-VNGPEILNKYVGESEANIRKLFADAee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 398 --RARAPC----IVYIDEIDAVGKKRStSMSGFSNTEEeQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPGRL 471
Cdd:cd19504    94 eqRRLGANsglhIIIFDEIDAICKQRG-SMAGSTGVHD-TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRL 171

                  ....*.
gi 2172663947 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 1.09e-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: 110.46  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 303 GKGVSFQDVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEV 381
Cdd:cd19525    16 GPPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 382 IGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGMGTA--DHVIVLASTNRAD 459
Cdd:cd19525    95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG----EHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQ 170
                         170
                  ....*....|....*...
gi 2172663947 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 2.27e-27

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 109.18  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 306 VSFQDVAGMHEAKLEVREFVDYlksPERFLQL--GAKVP-KGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVI 382
Cdd:cd19521     4 VKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 383 GGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSnteeEQTLNQLLVEMDGMGT-ADHVIVLASTNRADVL 461
Cdd:cd19521    81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEAS----RRIKTELLVQMNGVGNdSQGVLVLGATNIPWQL 156
                         170
                  ....*....|....*.
gi 2172663947 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 6.60e-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: 107.60  E-value: 6.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEA-----QVPFLAMAGPEFVEVIG 383
Cdd:cd19517     1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 384 GLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTeeeqTLNQLLVEMDGMGTADHVIVLASTNRADVLDN 463
Cdd:cd19517    81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS----IVSTLLALMDGLDNRGQVVVIGATNRPDALDP 156
                         170
                  ....*....|
gi 2172663947 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 1.03e-26

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 106.86  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLGAKvPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19524     1 DIAGQDLAKQALQEMVILpSLRPELFTGLRAP-ARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSmsgfSNTEEEQTLNQLLVEMDGM--GTADHVIVLASTNRADVLDNALM 466
Cdd:cd19524    80 LVRALFAVARELQPSIIFIDEVDSLLSERSEG----EHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                         170
                  ....*....|.
gi 2172663947 467 RpgRLDRHVFI 477
Cdd:cd19524   156 R--RFTKRVYV 164
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
310-467 6.69e-26

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 104.81  E-value: 6.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLG-AKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19520     1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 388 ARVRSLFKEARARAPCIVYIDEIDAVGKKRSTsmsgfsnTEEEQTL---NQLLVEMDGMGTADH--VIVLASTNRADVLD 462
Cdd:cd19520    81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSS-------TDHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLD 153

                  ....*
gi 2172663947 463 NALMR 467
Cdd:cd19520   154 EAILR 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
312-479 3.37e-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: 3.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 312 AGMHEAKLEVREFVDYlksperflqlgaKVPKGALLLGPPGCGKTLLAKAVATEA---QVPFLAMAGPEFVE---VIGGL 385
Cdd:cd00009     1 VGQEEAIEALREALEL------------PPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEglvVAELF 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 386 GAARVRSLFKEARARAPCIVYIDEIDAVGKKrstsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNAL 465
Cdd:cd00009    69 GHFLVRLLFELAEKAKPGVLFIDEIDSLSRG-----------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                         170
                  ....*....|....
gi 2172663947 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 3.42e-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: 85.11  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAK--LEVREfVDYLKSPERFlqlGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGA 387
Cdd:cd19507     1 DVGGLDNLKdwLKKRK-AAFSKQASAY---GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 388 ARVRSLFKEARARAPCIVYIDEID-AVGKKRSTSMSGFSNteeeQTLNQLLVEMDGMGTAdhVIVLASTNRADVLDNALM 466
Cdd:cd19507    77 SRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSS----RVLGTFLTWLQEKKKP--VFVVATANNVQSLPPELL 150
                         170
                  ....*....|.
gi 2172663947 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 3.48e-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: 3.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 321 VREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfveviGGLGAARVRSLFKEARAR 400
Cdd:cd19510     2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPKQ 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 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 1.00e-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: 78.39  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDY-LKSPERFLQLgAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAA 388
Cdd:cd19523     1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 389 RVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEqtlnqLLVEMDGMGTA--DHVIVLASTNRADVLDNALM 466
Cdd:cd19523    80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSgeDGVLVVCTTSKPEEIDESLR 154

                  .
gi 2172663947 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 1.85e-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: 1.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947  342 PKGALLLGPPGCGKTLLAKAVATEAQVP---FLAMAGPEFVEVI--------------GGLGAARVRSLFKEARARAPCI 404
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEVldqllliivggkkaSGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2172663947  405 VYIDEIDAVGKKRStsmsgfsntEEEQTLNQLLVEMDGMGTADHVIVLASTNRADVLDNALMRPgRLDRHVFIDLPT 481
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
507-546 3.33e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.70  E-value: 3.33e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2172663947 507 QRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFE 546
Cdd:pfam17862   5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
335-473 1.18e-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: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 335 LQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMA-------GPEFVEVIGGLGAA-------RVRSLFKEARAR 400
Cdd:cd19505     5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynKPDFGNDDWIDGMLilkeslhRLNLQFELAKAM 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2172663947 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 1.36e-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: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEfVEVIGGLGAARVRSLFKEA-RARAPCIVYIDEIDAVGKKRSTS-MSg 423
Cdd:cd19512    26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEkIS- 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2172663947 424 fsnTEEEQTLNQLLVEMdGMGTADHVIVLAStNRADVLDNAL 465
Cdd:cd19512   104 ---EDLRAALNAFLYRT-GEQSNKFMLVLAS-NQPEQFDWAI 140
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
346-416 1.90e-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: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA---RARAPC-IVYIDEI 410
Cdd:COG1219   113 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydVEKAERgIIYIDEI 183

                  ....*.
gi 2172663947 411 DAVGKK 416
Cdd:COG1219   184 DKIARK 189
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
346-411 3.96e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 49.98  E-value: 3.96e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172663947 346 LLLGPPGCGKTLLAKAVAtEA--QVPFLAMAGPEFVEV--------IGGLGAARVRSLFKEArARAPCIVYIDEID 411
Cdd:pfam07728   3 LLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDTTEedlfgrrnIDPGGASWVDGPLVRA-AREGEIAVLDEIN 76
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
346-416 4.12e-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: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPF-------LAMAG--PEFVEVIgglgaarVRSLFKEAR---ARAP-CIVYIDEIDA 412
Cdd:cd19497    54 LLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAGyvGEDVENI-------LLKLLQAADydvERAQrGIVYIDEIDK 126

                  ....
gi 2172663947 413 VGKK 416
Cdd:cd19497   127 IARK 130
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
346-416 9.06e-07

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 52.08  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFlAMA-----------GpEFVEVIgglgaarVRSLFKEA-----RA-RApcIVYID 408
Cdd:PRK05342  112 LLIGPTGSGKTLLAQTLARILDVPF-AIAdattlteagyvG-EDVENI-------LLKLLQAAdydveKAqRG--IVYID 180

                  ....*...
gi 2172663947 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 2.39e-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: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 341 VPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVigGLGAARVRSLFKEArarAPCIVYIDEIDAVGKKRSTS 420
Cdd:cd19498    45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEV--GYVGRDVESIIRDL---VEGIVFIDEIDKIAKRGGSS 119
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
346-410 4.62e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 49.70  E-value: 4.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:PRK13342   40 ILWGPPGTGKTTLARIIAGATDAPFEALSA-----VTSGV--KDLREVIEEARQRRsagrRTILFIDEI 101
PRK04195 PRK04195
replication factor C large subunit; Provisional
307-411 5.69e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 49.53  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 307 SFQDVAGMHEAKLEVREFVdylkspERFLQlgaKVPKGALLL-GPPGCGKTLLAKAVATEaqvpflamAGPEFVE----- 380
Cdd:PRK04195   12 TLSDVVGNEKAKEQLREWI------ESWLK---GKPKKALLLyGPPGVGKTSLAHALAND--------YGWEVIElnasd 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2172663947 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 7.25e-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: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 145 LFIIAIVMSLLNSLSTSGGS----ISWADFVNeMLAKGEVQRVQVVPESDVVEVYLHPGAVVfGRPRLAlMYRMQVANID 220
Cdd:pfam06480   5 LLILLVLLLLFLLFLLSSSSstkeISYSEFLE-YLEAGKVKKVVVQDDEILPTGVVEGTLKD-GSKFTT-YFIPSLPNVD 81
                          90       100
                  ....*....|....*....|..
gi 2172663947 221 KFEEKLRAAEDELNIESKDRIP 242
Cdd:pfam06480  82 SLLEKLEDALEEKGVKVSVKPP 103
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
346-410 8.07e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.90  E-value: 8.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGpefveVIGGLgaARVRSLFKEARARA----PCIVYIDEI 410
Cdd:COG2256    53 ILWGPPGTGKTTLARLIANATDAEFVALSA-----VTSGV--KDIREVIEEARERRaygrRTILFVDEI 114
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
343-378 2.15e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.58  E-value: 2.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2172663947 343 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 378
Cdd:COG1224    65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
310-415 6.62e-04

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.39  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 310 DVAGMHEAKLEVREFVDYLKsperflqLGAKVpKGALLL--GPPGCGKTLLAKAVATeaqvpflAMaGPEFVEV-IGGL- 385
Cdd:cd19500    11 DHYGLEDVKERILEYLAVRK-------LKGSM-KGPILClvGPPGVGKTSLGKSIAR-------AL-GRKFVRIsLGGVr 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2172663947 386 -------------GA--ARVRSLFKEARARAPCIVyIDEIDAVGK 415
Cdd:cd19500    75 deaeirghrrtyvGAmpGRIIQALKKAGTNNPVFL-LDEIDKIGS 118
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
343-378 8.41e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 42.30  E-value: 8.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2172663947 343 KGALLLGPPGCGKTLLAKAVATE--AQVPFLAMAGPEF 378
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
346-554 2.39e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.54  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPF-------------------LAMAGPEFVEVIGGLGAArvrslfkeararapcIVY 406
Cdd:COG0714    35 LLEGVPGVGKTTLAKALARALGLPFiriqftpdllpsdilgtyiYDQQTGEFEFRPGPLFAN---------------VLL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 407 IDEIDavgkkRSTsmsgfsnteeEQTLNQLLVEMD------GMGT---ADHVIVLASTNRADV-----LDNALmrpgrLD 472
Cdd:COG0714   100 ADEIN-----RAP----------PKTQSALLEAMEerqvtiPGGTyklPEPFLVIATQNPIEQegtypLPEAQ-----LD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 473 R---HVFIDLPTLQERREIFEQHLKGlkltqpssfysqRLAELTPGFSGADIAnicneAALHAAREGHtsVHTFNFEYAV 549
Cdd:COG0714   160 RfllKLYIGYPDAEEEREILRRHTGR------------HLAEVEPVLSPEELL-----ALQELVRQVH--VSEAVLDYIV 220

                  ....*
gi 2172663947 550 ERVIA 554
Cdd:COG0714   221 DLVRA 225
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
313-460 2.41e-03

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 41.37  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 313 GMHEAKLEVREFVDYLKSPERFLQLGAKVPKGA---LLLGPPGCGKTLLAKAVATeaqvpFLAMAG----PEFVEV---- 381
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAK-----IYCGLGvlrkPLVREVsrad 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 382 -IG---GLGAARVRSLFKEARARapcIVYIDEIDAVGKKRSTSMSGFSNteeeQTLNQLLVEMDgmGTADHVIVLASTNR 457
Cdd:TIGR03922 355 lIGqyiGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGL----EAIDTLLARME--NDRDRLVVIGAGYR 425

                  ...
gi 2172663947 458 ADV 460
Cdd:TIGR03922 426 KDL 428
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
343-410 3.94e-03

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 39.76  E-value: 3.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2172663947 343 KGALLLGPPGCGKTLLAKAVATEAqvpflAMAG--------PEFVEvigGLGAARV-RSLFKEAR--ARAPCIVyIDEI 410
Cdd:COG1484   100 ENLILLGPPGTGKTHLAIALGHEA-----CRAGyrvrfttaPDLVN---ELKEARAdGRLERLLKrlAKVDLLI-LDEL 169
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
346-463 4.20e-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: 37.87  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIgglgAARVRSLFKEARaraPCIVYIDEIdavgkkrSTSMSGFS 425
Cdd:cd01120     2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDTI----LEAIEDLIEEKK---LDIIIIDSL-------SSLARASQ 67
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2172663947 426 NTEEEQTLNQLLVEMDGMGTAdHVIVLASTNRADVLDN 463
Cdd:cd01120    68 GDRSSELLEDLAKLLRAARNT-GITVIATIHSDKFDID 104
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
346-376 4.74e-03

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.64  E-value: 4.74e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2172663947 346 LLLGPPGCGKTLLAKAVATEAQVPFLAMAGP 376
Cdd:pfam05496  37 LLYGPPGLGKTTLANIIANEMGVNIRITSGP 67
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
308-364 9.17e-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: 9.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2172663947 308 FQDVAGMHEAK--LEVrefvdylksperflqlgakvpkgA-------LLLGPPGCGKTLLAKAVAT 364
Cdd:COG0606   191 LADVKGQEQAKraLEI-----------------------AaagghnlLMIGPPGSGKTMLARRLPG 233
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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