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Conserved domains on  [gi|22329400|ref|NP_172231|]
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FTSH protease 10 [Arabidopsis thaliana]

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];
143-763 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 785.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 143 LMAIALILSTFSLGSREQQQISFQEFKNklleaglvdhiDVSNKEVAKVYVrsspksqtTEEVVQGPGNGvpakgrGGQY 222
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-----------LVEAGKVKSVTI--------QGDRITGTLKD------GTKT 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 223 KYYFNIGSVESFEEKLEEAQeaigvnshdfVPVTYVSET---IWYQELLRFAPTLLLVATLIFGARRMQGGLGGlggpgg 299
Cdd:COG0465  57 RFTTYRVNDPELVDLLEEKG----------VEVTAKPPEessWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------ 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 300 kagrgIFNIGKAQITRADKNsKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKA 379
Cdd:COG0465 121 -----AMSFGKSKAKLYDED-KPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKA 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 380 TAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMD 459
Cdd:COG0465 195 VAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMD 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 460 GFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADI 539
Cdd:COG0465 274 GFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADL 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 540 ANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGt 619
Cdd:COG0465 352 ANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG- 430
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 620 AALGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVLIGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQRE 698
Cdd:COG0465 431 RALGYTMQLPEEDrYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE 510
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329400 699 DE--------FSKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGE 763
Cdd:COG0465 511 GEvflgrdigQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
143-763 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 785.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 143 LMAIALILSTFSLGSREQQQISFQEFKNklleaglvdhiDVSNKEVAKVYVrsspksqtTEEVVQGPGNGvpakgrGGQY 222
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-----------LVEAGKVKSVTI--------QGDRITGTLKD------GTKT 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 223 KYYFNIGSVESFEEKLEEAQeaigvnshdfVPVTYVSET---IWYQELLRFAPTLLLVATLIFGARRMQGGLGGlggpgg 299
Cdd:COG0465  57 RFTTYRVNDPELVDLLEEKG----------VEVTAKPPEessWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------ 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 300 kagrgIFNIGKAQITRADKNsKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKA 379
Cdd:COG0465 121 -----AMSFGKSKAKLYDED-KPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKA 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 380 TAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMD 459
Cdd:COG0465 195 VAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMD 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 460 GFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADI 539
Cdd:COG0465 274 GFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADL 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 540 ANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGt 619
Cdd:COG0465 352 ANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG- 430
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 620 AALGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVLIGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQRE 698
Cdd:COG0465 431 RALGYTMQLPEEDrYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE 510
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329400 699 DE--------FSKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGE 763
Cdd:COG0465 511 GEvflgrdigQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
263-762 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: 703.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   263 WYQELLRFAPTLLLVATLIFGARRMQGGLGGLggpggkagrgIFNIGKAQiTRADKNSKNKIYFKDVAGCEEAKQEIMEF 342
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGVWFFFRRQMQGGGGR----------AFSFGKSK-AKLLNEEKPKVTFKDVAGIDEAKEELMEI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   343 VHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSI 422
Cdd:TIGR01241  71 VDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   423 IFIDEIDAIGRARGRgGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKG 502
Cdd:TIGR01241 151 IFIDEIDAVGRQRGA-GLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   503 RDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVIS 582
Cdd:TIGR01241 230 REEILKVHAKNKKLAPDVDL--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVIS 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   583 KLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTaALGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVLIGRI 661
Cdd:TIGR01241 308 EKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDkYLYTKSQLLAQIAVLLGGRAAEEIIFGEV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   662 STGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEF--------SKPYSNRTGAMIDEEVREWVGKAYKRTVELIE 733
Cdd:TIGR01241 387 TTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDVflgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILT 466
                         490       500
                  ....*....|....*....|....*....
gi 22329400   734 EHKEQVAQIAELLLEKEVLHQDDLTKVLG 762
Cdd:TIGR01241 467 ENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
236-764 9.12e-169

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 502.27  E-value: 9.12e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  236 EKLEEAQeaIGVNSHdfvPVtyVSETIWYQELLRFAPTLLLVATLIFGARRmqgglggLGGPGGKAGRGIFNIGKAQiTR 315
Cdd:CHL00176 107 QKLKEAN--IDFDAH---PP--VLKSNIVTILSNLLLPLILIGVLWFFFQR-------SSNFKGGPGQNLMNFGKSK-AR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  316 ADKNSKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSD 395
Cdd:CHL00176 172 FQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  396 FMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRgGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNR 475
Cdd:CHL00176 252 FVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGA-GIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  476 PDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEG 555
Cdd:CHL00176 331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSL--ELIARRTPGFSGADLANLLNEAAILTARRKK 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  556 ATVTMAHFDSAIDRVIGGLEKKNRVISKLeRRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGtAALGFAQYVPNE-NLL 634
Cdd:CHL00176 409 ATITMKEIDTAIDRVIAGLEGTPLEDSKN-KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPEEdQSL 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  635 MTKEQLFDMTCMTLGGRAAEQVLIG--RISTGAQNDLEKVTKMTYAQVAVYGFSdKIGLLS---------FPQREDEFSK 703
Cdd:CHL00176 487 VSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISlesnnstdpFLGRFMQRNS 565
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329400  704 PYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGER 764
Cdd:CHL00176 566 EYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSY 626
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
324-495 2.24e-112

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: 339.21  E-value: 2.24e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 324 IYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGV 403
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 404 GPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKAL 483
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGL-GGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 22329400 484 LRPGRFDRQITI 495
Cdd:cd19501 160 LRPGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
579-760 1.59e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.55  E-value: 1.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   579 RVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTAaLGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVL 657
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   658 IGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEF--------SKPYSNRTGAMIDEEVREWVGKAYKRTV 729
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVflgrgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 22329400   730 ELIEEHKEQVAQIAELLLEKEVLHQDDLTKV 760
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
360-499 6.37e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 81.27  E-value: 6.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400    360 PKGALLVGPPGTGKTLLAKATAGESAVP---FLSISGSDFME--------------MFVGVGPSRVRNLFQEARQCAPSI 422
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329400    423 IFIDEIDAIGRARGrggfsggndERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPgRFDRQITIDKPD 499
Cdd:smart00382  82 LILDEITSLLDAEQ---------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
143-763 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 785.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 143 LMAIALILSTFSLGSREQQQISFQEFKNklleaglvdhiDVSNKEVAKVYVrsspksqtTEEVVQGPGNGvpakgrGGQY 222
Cdd:COG0465   2 ALLLVLLFNLFSSSSSSVKEISYSEFLQ-----------LVEAGKVKSVTI--------QGDRITGTLKD------GTKT 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 223 KYYFNIGSVESFEEKLEEAQeaigvnshdfVPVTYVSET---IWYQELLRFAPTLLLVATLIFGARRMQGGLGGlggpgg 299
Cdd:COG0465  57 RFTTYRVNDPELVDLLEEKG----------VEVTAKPPEessWLLSLLISLLPILLLIGLWIFFMRRMQGGGGG------ 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 300 kagrgIFNIGKAQITRADKNsKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKA 379
Cdd:COG0465 121 -----AMSFGKSKAKLYDED-KPKVTFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKA 194
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 380 TAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMD 459
Cdd:COG0465 195 VAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGL-GGGHDEREQTLNQLLVEMD 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 460 GFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADI 539
Cdd:COG0465 274 GFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL--EVIARRTPGFSGADL 351
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 540 ANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGt 619
Cdd:COG0465 352 ANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTIIPRG- 430
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 620 AALGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVLIGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQRE 698
Cdd:COG0465 431 RALGYTMQLPEEDrYLYTKEELLDRIAVLLGGRAAEELVFGEVTTGASNDLERATKIARAMVTEYGMSEKLGPVAYGESE 510
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22329400 699 DE--------FSKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGE 763
Cdd:COG0465 511 GEvflgrdigQSRNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEILAG 583
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
263-762 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: 703.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   263 WYQELLRFAPTLLLVATLIFGARRMQGGLGGLggpggkagrgIFNIGKAQiTRADKNSKNKIYFKDVAGCEEAKQEIMEF 342
Cdd:TIGR01241   2 LLGFLFSLLPPILLLVGVWFFFRRQMQGGGGR----------AFSFGKSK-AKLLNEEKPKVTFKDVAGIDEAKEELMEI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   343 VHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSI 422
Cdd:TIGR01241  71 VDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   423 IFIDEIDAIGRARGRgGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKG 502
Cdd:TIGR01241 151 IFIDEIDAVGRQRGA-GLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKG 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   503 RDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVIS 582
Cdd:TIGR01241 230 REEILKVHAKNKKLAPDVDL--KAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVIS 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   583 KLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTaALGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVLIGRI 661
Cdd:TIGR01241 308 EKEKKLVAYHEAGHALVGLLLKDADPVHKVTIIPRGQ-ALGYTQFLPEEDkYLYTKSQLLAQIAVLLGGRAAEEIIFGEV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   662 STGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEF--------SKPYSNRTGAMIDEEVREWVGKAYKRTVELIE 733
Cdd:TIGR01241 387 TTGASNDIKQATNIARAMVTEWGMSDKLGPVAYGSDGGDVflgrgfakAKEYSEETAREIDEEVKRIIEEAYKRAKQILT 466
                         490       500
                  ....*....|....*....|....*....
gi 22329400   734 EHKEQVAQIAELLLEKEVLHQDDLTKVLG 762
Cdd:TIGR01241 467 ENRDELELLAKALLEKETITREEIKELLA 495
ftsH CHL00176
cell division protein; Validated
236-764 9.12e-169

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 502.27  E-value: 9.12e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  236 EKLEEAQeaIGVNSHdfvPVtyVSETIWYQELLRFAPTLLLVATLIFGARRmqgglggLGGPGGKAGRGIFNIGKAQiTR 315
Cdd:CHL00176 107 QKLKEAN--IDFDAH---PP--VLKSNIVTILSNLLLPLILIGVLWFFFQR-------SSNFKGGPGQNLMNFGKSK-AR 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  316 ADKNSKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSD 395
Cdd:CHL00176 172 FQMEADTGITFRDIAGIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  396 FMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRgGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNR 475
Cdd:CHL00176 252 FVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGA-GIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  476 PDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEG 555
Cdd:CHL00176 331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSL--ELIARRTPGFSGADLANLLNEAAILTARRKK 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  556 ATVTMAHFDSAIDRVIGGLEKKNRVISKLeRRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGtAALGFAQYVPNE-NLL 634
Cdd:CHL00176 409 ATITMKEIDTAIDRVIAGLEGTPLEDSKN-KRLIAYHEVGHAIVGTLLPNHDPVQKVTLIPRG-QAKGLTWFTPEEdQSL 486
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  635 MTKEQLFDMTCMTLGGRAAEQVLIG--RISTGAQNDLEKVTKMTYAQVAVYGFSdKIGLLS---------FPQREDEFSK 703
Cdd:CHL00176 487 VSRSQILARIVGALGGRAAEEVVFGstEVTTGASNDLQQVTNLARQMVTRFGMS-SIGPISlesnnstdpFLGRFMQRNS 565
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329400  704 PYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGER 764
Cdd:CHL00176 566 EYSEEIADKIDMEVRSILHTCYQYAYQILKDNRVLIDLLVELLLQKETIDGDEFREIVNSY 626
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
272-773 6.85e-151

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 456.42  E-value: 6.85e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  272 PTLLLVATLIFGARRMQGGLGGLGGPggkagrgiFNIGKAQITRADKNsknKIYFKDVAGCEEAKQEIMEFVHFLQNPKK 351
Cdd:PRK10733 108 PMLLLIGVWIFFMRQMQGGGGKGAMS--------FGKSKARMLTEDQI---KTTFADVAGCDEAKEEVAELVEYLREPSR 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  352 YEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAI 431
Cdd:PRK10733 177 FQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAV 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  432 GRARGrGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYL 511
Cdd:PRK10733 257 GRQRG-AGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHM 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  512 KKIKLDhePSYYSQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAY 591
Cdd:PRK10733 336 RRVPLA--PDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAY 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  592 HESGHAVAGWFLEHAEPLLKVTIVPRGTaALGFAQYVPNENLLMTKEQLFDMTCMTL-GGRAAEQVLIG--RISTGAQND 668
Cdd:PRK10733 414 HEAGHAIIGRLVPEHDPVHKVTIIPRGR-ALGVTFFLPEGDAISASRQKLESQISTLyGGRLAEEIIYGpeHVSTGASND 492
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  669 LEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEF--------SKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVA 740
Cdd:PRK10733 493 IKVATNLARNMVTQWGFSEKLGPLLYAEEEGEVflgrsvakAKHMSDETARIIDQEVKALIERNYNRARQLLTDNMDILH 572
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 22329400  741 QIAELLLEKEVLHQ---DDLTKVLGERPFKSGETTN 773
Cdd:PRK10733 573 AMKDALMKYETIDApqiDDLMARRDVRPPAGWEEPG 608
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
324-495 2.24e-112

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: 339.21  E-value: 2.24e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 324 IYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGV 403
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 404 GPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKAL 483
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGL-GGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 22329400 484 LRPGRFDRQITI 495
Cdd:cd19501 160 LRPGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
311-577 6.62e-103

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 320.41  E-value: 6.62e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 311 AQITRADKNSKNKIYFKDVAGCEEAKQEIMEFV-HFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFL 389
Cdd:COG1222  62 TPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVeLPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 390 SISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSGgndERESTLNQLLVEMDGFGTTAGVVV 469
Cdd:COG1222 142 RVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSG---EVQRTVNQLLAELDGFESRGDVLI 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 470 LAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALI 549
Cdd:COG1222 219 IAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL--DKLAKLTEGFSGADLKAIVTEAGMF 296
                       250       260
                ....*....|....*....|....*...
gi 22329400 550 AARHEGATVTMAHFDSAIDRVIGGLEKK 577
Cdd:COG1222 297 AIREGRDTVTMEDLEKAIEKVKKKTETA 324
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
323-578 1.02e-86

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 280.18  E-value: 1.02e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  323 KIYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFV 401
Cdd:PRK03992 127 NVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  402 GVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSGgndERE--STLNQLLVEMDGFGTTAGVVVLAGTNRPDIL 479
Cdd:PRK03992 207 GEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSG---DREvqRTLMQLLAEMDGFDPRGNVKIIAATNRIDIL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  480 DKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVT 559
Cdd:PRK03992 284 DPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL--EELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*....
gi 22329400  560 MAHFDSAIDRVIGGLEKKN 578
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDS 380
Peptidase_M41 pfam01434
Peptidase family M41;
579-760 1.59e-86

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 272.55  E-value: 1.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   579 RVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTAaLGFAQYVPNEN-LLMTKEQLFDMTCMTLGGRAAEQVL 657
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQA-LGYTQFLPEEDkLLYTKEQLLARIAVLLGGRAAEELI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   658 IGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEF--------SKPYSNRTGAMIDEEVREWVGKAYKRTV 729
Cdd:pfam01434  80 FGEVTTGASNDLEKATKIARQMVTEFGMSDKLGPVSLEESDGNVflgrgmgkRKPYSEETADIIDEEVKRLLEEAYERAK 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 22329400   730 ELIEEHKEQVAQIAELLLEKEVLHQDDLTKV 760
Cdd:pfam01434 160 EILTEHRDELEALAEALLEKETLDAEEIREL 190
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
326-570 1.49e-79

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: 261.77  E-value: 1.49e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 326 FKDVAGCEEAKQEIMEFV-HFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVG 404
Cdd:COG0464 156 LDDLGGLEEVKEELRELVaLPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 405 PSRVRNLFQEARQCAPSIIFIDEIDAIgrARGRGGFSGGNDEREstLNQLLVEMDGFgtTAGVVVLAGTNRPDILDKALL 484
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADAL--AGKRGEVGDGVGRRV--VNTLLTEMEEL--RSDVVVIAATNRPDLLDPALL 309
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 485 RpgRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFD 564
Cdd:COG0464 310 R--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDL--EELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385

                ....*.
gi 22329400 565 SAIDRV 570
Cdd:COG0464 386 EALERE 391
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
321-571 2.36e-75

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 249.33  E-value: 2.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   321 KNKIYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEM 399
Cdd:TIGR01242 116 RPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRK 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   400 FVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDIL 479
Cdd:TIGR01242 196 YIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSG-TSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDIL 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   480 DKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVT 559
Cdd:TIGR01242 275 DPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDL--EAIAKMTEGASGADLKAICTEAGMFAIREERDYVT 352
                         250
                  ....*....|..
gi 22329400   560 MAHFDSAIDRVI 571
Cdd:TIGR01242 353 MDDFIKAVEKVL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
324-586 9.21e-66

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: 233.26  E-value: 9.21e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   324 IYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVG 402
Cdd:TIGR01243 450 VRWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVG 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   403 VGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRggfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKA 482
Cdd:TIGR01243 530 ESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGA---RFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPA 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   483 LLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGAT----- 557
Cdd:TIGR01243 607 LLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL--EELAEMTEGYTGADIEAVCREAAMAALRESIGSpakek 684
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 22329400   558 -------------VTMAHFDSAIDRVIGGLEKKN-RVISKLER 586
Cdd:TIGR01243 685 levgeeeflkdlkVEMRHFLEALKKVKPSVSKEDmLRYERLAK 727
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
326-495 1.24e-62

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: 207.96  E-value: 1.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 326 FKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVG 404
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 405 PSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALL 484
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSG-TGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                       170
                ....*....|.
gi 22329400 485 RPGRFDRQITI 495
Cdd:cd19502 161 RPGRFDRKIEF 171
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
335-495 5.95e-62

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: 205.59  E-value: 5.95e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 335 AKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQE 414
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 415 ARQCAPSIIFIDEIDAIGRARGRggfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQIT 494
Cdd:cd19481  81 ARRLAPCILFIDEIDAIGRKRDS---SGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                .
gi 22329400 495 I 495
Cdd:cd19481 158 F 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
326-571 5.37e-60

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 210.01  E-value: 5.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  326 FKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVG 404
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  405 PSRVRNLFQEARQCAPSIIFIDEIDAIGRARgRGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALL 484
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKR-YDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  485 RPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFD 564
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDL--EEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQADFR 418

                 ....*..
gi 22329400  565 SAIDRVI 571
Cdd:PTZ00361 419 KAKEKVL 425
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
326-569 4.36e-59

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 201.27  E-value: 4.36e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 326 FKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGP 405
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 406 SRVRNLFQEARQcAPSIIFIDEIDAIGRARgrgGFSGGNDERESTLNQLLVEMDGFgtTAGVVVLAGTNRPDILDKALLR 485
Cdd:COG1223  81 RNLRKLFDFARR-APCVIFFDEFDAIAKDR---GDQNDVGEVKRVVNALLQELDGL--PSGSVVIAATNHPELLDSALWR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 486 pgRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEpsYYSQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDS 565
Cdd:COG1223 155 --RFDEVIEFPLPDKEERKEILELNLKKFPLPFE--LDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEE 230

                ....
gi 22329400 566 AIDR 569
Cdd:COG1223 231 ALKQ 234
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
335-495 5.68e-58

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: 194.81  E-value: 5.68e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 335 AKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQ 413
Cdd:cd19511   1 VKRELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 414 EARQCAPSIIFIDEIDAIGRARGrGGFSGGNDEResTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQI 493
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRG-QSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157

                ..
gi 22329400 494 TI 495
Cdd:cd19511 158 YV 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
311-571 8.84e-57

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 199.99  E-value: 8.84e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  311 AQITRADKNSKNKIYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFL 389
Cdd:PTZ00454 129 SSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFI 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  390 SISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARgrggF---SGGNDERESTLNQLLVEMDGFGTTAG 466
Cdd:PTZ00454 209 RVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR----FdaqTGADREVQRILLELLNQMDGFDQTTN 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  467 VVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEA 546
Cdd:PTZ00454 285 VKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDL--EDFVSRPEKISAADIAAICQEA 362
                        250       260
                 ....*....|....*....|....*
gi 22329400  547 ALIAARHEGATVTMAHFDSAIDRVI 571
Cdd:PTZ00454 363 GMQAVRKNRYVILPKDFEKGYKTVV 387
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
328-495 1.02e-55

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: 189.04  E-value: 1.02e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPS 406
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 407 RVRNLFQEARQCAPSIIFIDEIDAIGRARGrggfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRP 486
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKRE----EDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                ....*....
gi 22329400 487 GRFDRQITI 495
Cdd:cd19503 157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
323-552 1.53e-55

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: 204.37  E-value: 1.53e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   323 KIYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFV 401
Cdd:TIGR01243 174 KVTYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYY 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   402 GVGPSRVRNLFQEARQCAPSIIFIDEIDAIgrARGRGGFSGGNDEResTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDK 481
Cdd:TIGR01243 254 GESEERLREIFKEAEENAPSIIFIDEIDAI--APKREEVTGEVEKR--VVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329400   482 ALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYysQRLAALTPGFAGADIANVCNEAALIAAR 552
Cdd:TIGR01243 330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL--DKLAEVTHGFVGADLAALAKEAAMAALR 398
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
335-495 1.11e-53

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: 183.08  E-value: 1.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 335 AKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQ 413
Cdd:cd19529   1 VKQELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 414 EARQCAPSIIFIDEIDAIGRARGRGGFSGGNDEresTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQI 493
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTER---VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157

                ..
gi 22329400 494 TI 495
Cdd:cd19529 158 YI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
336-495 4.03e-50

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: 173.47  E-value: 4.03e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 336 KQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQE 414
Cdd:cd19528   2 KRELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 415 ARQCAPSIIFIDEIDAIGRARGrGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQIT 494
Cdd:cd19528  82 ARAAAPCVLFFDELDSIAKARG-GNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 22329400 495 I 495
Cdd:cd19528 161 I 161
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
364-496 6.01e-50

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: 171.62  E-value: 6.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   364 LLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSgg 443
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS-- 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22329400   444 ndERESTLNQLLVEMDGF-GTTAGVVVLAGTNRPDILDKALLrpGRFDRQITID 496
Cdd:pfam00004  80 --ESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
328-495 1.83e-48

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: 168.77  E-value: 1.83e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPS 406
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 407 RVRNLFQEARQCAPSIIFIDEIDAIGRARGRggfSGGNDEREsTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRP 486
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK---THGEVERR-IVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156

                ....*....
gi 22329400 487 GRFDRQITI 495
Cdd:cd19519 157 GRFDREIDI 165
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
336-491 5.59e-47

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: 164.58  E-value: 5.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 336 KQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEA 415
Cdd:cd19530   6 EELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRA 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329400 416 RQCAPSIIFIDEIDAIGRARGRGGFSGGnderESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDR 491
Cdd:cd19530  86 RASAPCVIFFDEVDALVPKRGDGGSWAS----ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
336-491 5.40e-43

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: 153.44  E-value: 5.40e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 336 KQEIMEFVhflQNPKKYEDL---GAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLF 412
Cdd:cd19527   2 KKEILDTI---QLPLEHPELfssGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 413 QEARQCAPSIIFIDEIDAIGRARGRGGFSGGNDEResTLNQLLVEMDGFGTTA-GVVVLAGTNRPDILDKALLRPGRFDR 491
Cdd:cd19527  79 QKARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDR--VVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
328-495 2.47e-42

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: 151.79  E-value: 2.47e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFV-HFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPS 406
Cdd:cd19518   1 DIGGMDSTLKELCELLiHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 407 RVRNLFQEARQCAPSIIFIDEIDAIGRARGrggfSGGNDERESTLNQLLVEMDGFG----TTAGVVVLAGTNRPDILDKA 482
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRE----SAQREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPA 156
                       170
                ....*....|...
gi 22329400 483 LLRPGRFDRQITI 495
Cdd:cd19518 157 LRRAGRFDREICL 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
349-493 6.48e-40

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: 144.49  E-value: 6.48e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 349 PKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEI 428
Cdd:cd19526  16 PKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPCILFFDEF 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329400 429 DAIgrARGRGGFSGGNDEResTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQI 493
Cdd:cd19526  96 DSI--APKRGHDSTGVTDR--VVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
329-495 2.42e-39

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: 142.88  E-value: 2.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 329 VAGCEEAKQEIMEFVHFlqnPKKYEDL---GAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGP 405
Cdd:cd19509   1 IAGLDDAKEALKEAVIL---PSLRPDLfpgLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 406 SRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGgfsggndERESTL---NQLLVEMDGFGTTA--GVVVLAGTNRPDILD 480
Cdd:cd19509  78 KIVRALFALARELQPSIIFIDEIDSLLSERGSG-------EHEASRrvkTEFLVQMDGVLNKPedRVLVLGATNRPWELD 150
                       170
                ....*....|....*
gi 22329400 481 KALLRpgRFDRQITI 495
Cdd:cd19509 151 EAFLR--RFEKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
321-495 3.30e-37

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: 137.30  E-value: 3.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 321 KNKIYFKDVAGCEEAKQEIMEFVHFlqnPKKYEDL--GAKIP-KGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFM 397
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVIL---PVKFPHLftGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 398 EMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGgfsggndERESTL---NQLLVEMDGFGT-TAGVVVLAGT 473
Cdd:cd19521  78 SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG-------ESEASRrikTELLVQMNGVGNdSQGVLVLGAT 150
                       170       180
                ....*....|....*....|..
gi 22329400 474 NRPDILDKALLRpgRFDRQITI 495
Cdd:cd19521 151 NIPWQLDSAIRR--RFEKRIYI 170
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
328-492 3.74e-33

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: 125.70  E-value: 3.74e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATA-----GESAVPFLSISGSDFMEMFV 401
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 402 GVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGrggfSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDK 481
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRS----SKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDP 156
                       170
                ....*....|.
gi 22329400 482 ALLRPGRFDRQ 492
Cdd:cd19517 157 ALRRPGRFDRE 167
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
328-489 1.26e-32

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: 124.07  E-value: 1.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEDLG-AKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGP 405
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 406 SRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGgfsggndERESTL---NQLLVEMDGFGTTAG--VVVLAGTNRPDILD 480
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST-------DHEATAmmkAEFMSLWDGLSTDGNcrVIVMGATNRPQDLD 153
                       170
                ....*....|.
gi 22329400 481 KALLR--PGRF 489
Cdd:cd19520 154 EAILRrmPKRF 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
328-495 2.26e-32

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: 123.04  E-value: 2.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHFlqnPKKYEDL--GAKIP-KGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVG 404
Cdd:cd19524   1 DIAGQDLAKQALQEMVIL---PSLRPELftGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 405 PSRVRNLFQEARQCAPSIIFIDEIDAIGRARGrggfSGGNDERESTLNQLLVEMDGFGTTAG--VVVLAGTNRPDILDKA 482
Cdd:cd19524  78 EKLVRALFAVARELQPSIIFIDEVDSLLSERS----EGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDA 153
                       170
                ....*....|...
gi 22329400 483 LLRpgRFDRQITI 495
Cdd:cd19524 154 VLR--RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
328-495 4.05e-32

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: 122.79  E-value: 4.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEdlGAKIP-KGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGP 405
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLpMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 406 SRVRNLFQEARQCAPSIIFIDEIDAIGRARgrggfsGGNDERESTL---NQLLVEMDGFGTTAG-------VVVLAGTNR 475
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR------GTSEEHEASRrvkSELLVQMDGVGGASEnddpskmVMVLAATNF 152
                       170       180
                ....*....|....*....|
gi 22329400 476 PDILDKALLRpgRFDRQITI 495
Cdd:cd19522 153 PWDIDEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
322-495 1.78e-31

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: 121.63  E-value: 1.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 322 NKIYFKDVAGCEEAKQEIMEFVHF-LQNPKKYEDLGAKiPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMF 400
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 401 VGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGgfsggndERESTL---NQLLVEMDGFGTTAG--VVVLAGTNR 475
Cdd:cd19525  96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEG-------EHESSRrikTEFLVQLDGATTSSEdrILVVGATNR 168
                       170       180
                ....*....|....*....|
gi 22329400 476 PDILDKALLRpgRFDRQITI 495
Cdd:cd19525 169 PQEIDEAARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
349-495 1.38e-29

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: 115.66  E-value: 1.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 349 PKKYEDLGAKIPKGALLVGPPGTGKTLLAKA-----TAGESAVpflsISGSDFMEMFVGVGPSRVRNLFQEA----RQCA 419
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQigkmlNAREPKI----VNGPEILNKYVGESEANIRKLFADAeeeqRRLG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 420 PS----IIFIDEIDAIGRARG-RGGFSGGNDereSTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQIT 494
Cdd:cd19504 100 ANsglhIIIFDEIDAICKQRGsMAGSTGVHD---TVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQME 176

                .
gi 22329400 495 I 495
Cdd:cd19504 177 I 177
ycf46 CHL00195
Ycf46; Provisional
350-550 9.03e-29

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 120.89  E-value: 9.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  350 KKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSIsgsDFMEMF---VGVGPSRVRNLFQEARQCAPSIIFID 426
Cdd:CHL00195 249 KQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRL---DVGKLFggiVGESESRMRQMIRIAEALSPCILWID 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  427 EID-AIGRARGRGGfSGGNDERESTLNQLLVEmdgfgTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQ 505
Cdd:CHL00195 326 EIDkAFSNSESKGD-SGTTNRVLATFITWLSE-----KKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREK 399
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 22329400  506 IFQIYLKKIKLDHEPSYYSQRLAALTPGFAGADIANVCNEAALIA 550
Cdd:CHL00195 400 IFKIHLQKFRPKSWKKYDIKKLSKLSNKFSGAEIEQSIIEAMYIA 444
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
360-497 2.07e-25

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: 102.99  E-value: 2.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 360 PKGALLVGPPGTGKTLLAKATAGESA---VPFLSISGSDFMEMFVG---VGPSRVRNLFQEARQCAPSIIFIDEIDAIGR 433
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELFrpgAPFLYLNASDLLEGLVVaelFGHFLVRLLFELAEKAKPGVLFIDEIDSLSR 98
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329400 434 argrggfsggnDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDK 497
Cdd:cd00009  99 -----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
356-491 1.85e-20

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: 88.96  E-value: 1.85e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 356 GAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAigrar 435
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEK----- 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329400 436 grgGFSGGNDERESTLNQLLvemdgFGT--------TAGVVVLAGTNRPDILDKALLRPGRFDR 491
Cdd:cd19507 102 ---GFSNADSKGDSGTSSRV-----LGTfltwlqekKKPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
339-493 4.25e-20

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: 87.79  E-value: 4.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 339 IMEFVH-FLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDfmemfVGVGPSRVRNLFQEARQ 417
Cdd:cd19510   1 IIDDLKdFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPK 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329400 418 caPSIIFIDEIDA--IGRARGRGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQI 493
Cdd:cd19510  76 --QSIILLEDIDAafESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
328-495 9.24e-19

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: 84.17  E-value: 9.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 328 DVAGCEEAKQEIMEFVHF-LQNPKKYEDLgAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPS 406
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWpLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 407 RVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSGGNDEREstlnqLLVEMDGFGTTA--GVVVLAGTNRPDILDKALL 484
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVGRLQVE-----LLAQLDGVLGSGedGVLVVCTTSKPEEIDESLR 154
                       170
                ....*....|.
gi 22329400 485 RpgRFDRQITI 495
Cdd:cd19523 155 R--YFSKRLLV 163
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
360-499 6.37e-18

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 81.27  E-value: 6.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400    360 PKGALLVGPPGTGKTLLAKATAGESAVP---FLSISGSDFME--------------MFVGVGPSRVRNLFQEARQCAPSI 422
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329400    423 IFIDEIDAIGRARGrggfsggndERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPgRFDRQITIDKPD 499
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 ...
525-565 2.18e-10

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: 56.39  E-value: 2.18e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 22329400   525 QRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDS 565
Cdd:pfam17862   5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
PRK04195 PRK04195
replication factor C large subunit; Provisional
326-439 2.45e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 63.79  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  326 FKDVAGCEEAKQEIMEFVhflqnpKKYEDlgAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDF-----MEMF 400
Cdd:PRK04195  13 LSDVVGNEKAKEQLREWI------ESWLK--GKPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvIERV 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 22329400  401 VGVGpSRVRNLFQEARQcapsIIFIDEIDAI-GRArGRGG 439
Cdd:PRK04195  85 AGEA-ATSGSLFGARRK----LILLDEVDGIhGNE-DRGG 118
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
359-468 6.01e-10

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: 59.32  E-value: 6.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 359 IPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEM-FVGvgpsrvRNLFQEARQCAPSIIFIDEIDAIGrarGR 437
Cdd:cd19498  45 TPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVgYVG------RDVESIIRDLVEGIVFIDEIDKIA---KR 115
                        90       100       110
                ....*....|....*....|....*....|...
gi 22329400 438 GGFSGGNDERESTLNQLL--VEMDGFGTTAGVV 468
Cdd:cd19498 116 GGSSGPDVSREGVQRDLLpiVEGSTVSTKYGPV 148
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
364-483 7.46e-10

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: 58.31  E-value: 7.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 364 LLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGvGPSRVRNLFQEARQCAPS-IIFIDEIDAIGRARGRGGFSg 442
Cdd:cd19512  26 LFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTSRRGlLLFVDEADAFLRKRSTEKIS- 103
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 22329400 443 gNDEReSTLNQLLVEMdGFGTTAGVVVLAgTNRPDILDKAL 483
Cdd:cd19512 104 -EDLR-AALNAFLYRT-GEQSNKFMLVLA-SNQPEQFDWAI 140
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
355-495 5.28e-09

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 55.84  E-value: 5.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 355 LGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFM--------------EMFVGVGPSRVRNLFQEARQCAP 420
Cdd:cd19505   7 LGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 421 SIIFIDEIDAIGRARgrggfsGGNDEREST------LNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQIT 494
Cdd:cd19505  87 CIIWIPNIHELNVNR------STQNLEEDPklllglLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCIN 160

                .
gi 22329400 495 I 495
Cdd:cd19505 161 I 161
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
323-433 2.93e-08

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: 54.10  E-value: 2.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 323 KIYFKDVAGCEEAKQEIMEFVHFLqnpKKYEDLGAKIpkgALLVGPPGTGKTLLAKATAGESAVPFLSIS-G--SDFMEM 399
Cdd:cd19500   6 KVLDADHYGLEDVKERILEYLAVR---KLKGSMKGPI---LCLVGPPGVGKTSLGKSIARALGRKFVRISlGgvRDEAEI 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22329400 400 ------FVGVGPSRVRNLFQEARQCAPsIIFIDEIDAIGR 433
Cdd:cd19500  80 rghrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEIDKIGS 118
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
364-431 8.93e-08

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 52.58  E-value: 8.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   364 LLVGPPGTGKTLLAKATAGE---SAVPFLSISGSDFME-----MFVGVGPSRVR-----NLFQEARQCAPSIIFIDEIDA 430
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEehsvsRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIEK 86

                  .
gi 22329400   431 I 431
Cdd:pfam07724  87 A 87
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
364-501 2.60e-07

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 51.68  E-value: 2.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 364 LLVGPPGTGKTLLAKATAGEsavpfLSI---------------SGSDFMEMFVGVGpSRVRNLFQEARQCAP---SIIF- 424
Cdd:cd19508  56 LLHGPPGTGKTSLCKALAQK-----LSIrlssryrygqlieinSHSLFSKWFSESG-KLVTKMFQKIQELIDdkdALVFv 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 425 -IDEIDAIGRArgRGGFSGGNDERES--TLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALlrpgrfdrqitIDKPDIK 501
Cdd:cd19508 130 lIDEVESLAAA--RSASSSGTEPSDAirVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF-----------VDRADIK 196
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
364-428 3.36e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.55  E-value: 3.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329400  364 LLVGPPGTGKTLLAKATAGESAVPFLSISGSdfmemFVGVgpSRVRNLFQEARQCAPS----IIFIDEI 428
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSAV-----TSGV--KDLREVIEEARQRRSAgrrtILFIDEI 101
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
329-433 6.47e-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: 51.45  E-value: 6.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 329 VAGCEEAKQEIMEFV--HF--LQNPKKYEDLGAKIPKG-ALLVGPPGTGKTLLAKATAGESAVPF-------LSISGsdf 396
Cdd:cd19497  14 VIGQERAKKVLSVAVynHYkrIRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFaiadattLTEAG--- 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 22329400 397 memFVGvgpSRVRN----LFQEA----RQCAPSIIFIDEIDAIGR 433
Cdd:cd19497  91 ---YVG---EDVENillkLLQAAdydvERAQRGIVYIDEIDKIAR 129
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
367-428 1.12e-06

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 51.98  E-value: 1.12e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329400 367 GPPGTGKTLLAKATAGESAVPFLSISGSdfmemFVGVgpSRVRNLFQEARQCA----PSIIFIDEI 428
Cdd:COG2256  56 GPPGTGKTTLARLIANATDAEFVALSAV-----TSGV--KDIREVIEEARERRaygrRTILFVDEI 114
FtsH_ext pfam06480
FtsH Extracellular; This domain is found in the FtsH family of proteins. FtsH is the only ...
139-254 1.81e-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: 47.21  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   139 MLIPLMAIALILSTFSLGSREQQQISFQEFKNKlLEAGLVDHIDVSNKEVakvyvrsspksqtteeVVQGPGNGVPAKGR 218
Cdd:pfam06480   5 LLILLVLLLLFLLFLLSSSSSTKEISYSEFLEY-LEAGKVKKVVVQDDEI----------------LPTGVVEGTLKDGS 67
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22329400   219 GGQYKYYFNIGSVESFEEKLEEAQEAIGVNSHDFVP 254
Cdd:pfam06480  68 KFTTYFIPSLPNVDSLLEKLEDALEEKGVKVSVKPP 103
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
361-397 4.78e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.97  E-value: 4.78e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 22329400 361 KGALLVGPPGTGKTLLAKATAGE--SAVPFLSISGSDFM 397
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIY 103
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
364-480 9.68e-06

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: 45.57  E-value: 9.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 364 LLVGPPGTGKTLLAKATAG---ESAVPFLSISgsdFMEMFvgvgpsrVRNLFQEARQCAPSIIFIDEIDAIGRARgrggf 440
Cdd:cd01120   2 LITGPPGSGKTTLLLQFAEqalLSDEPVIFIS---FLDTI-------LEAIEDLIEEKKLDIIIIDSLSSLARAS----- 66
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 22329400 441 sgGNDERESTLNQLLVEMdGFGTTAGVVVLAGTNRPDILD 480
Cdd:cd01120  67 --QGDRSSELLEDLAKLL-RAARNTGITVIATIHSDKFDI 103
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
364-489 2.50e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   364 LLVGPPGTGKT----LLAKATAGesaVPFLSISGSDFM---EMFvgvGPSRVRN---------LFQEARQcaPSIIFIDE 427
Cdd:pfam07728   3 LLVGPPGTGKTelaeRLAAALSN---RPVFYVQLTRDTteeDLF---GRRNIDPggaswvdgpLVRAARE--GEIAVLDE 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22329400   428 IDaigRArgrggfsggNDERESTLNQLLVE-----MDGFGTT----AGVVVLAGTNRPDI----LDKALLRpgRF 489
Cdd:pfam07728  75 IN---RA---------NPDVLNSLLSLLDErrlllPDGGELVkaapDGFRLIATMNPLDRglneLSPALRS--RF 135
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
364-429 3.21e-05

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 45.25  E-value: 3.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 364 LLVGPPGTGKTLLAKATA-----GESAvpFLSISGSDFMEMF-----VGVGPSRVRN-----LFQEARQCAPSIIFIDEI 428
Cdd:cd19499  45 LFLGPTGVGKTELAKALAellfgDEDN--LIRIDMSEYMEKHsvsrlIGAPPGYVGYteggqLTEAVRRKPYSVVLLDEI 122

                .
gi 22329400 429 D 429
Cdd:cd19499 123 E 123
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
361-396 8.70e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 8.70e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 22329400   361 KGALLVGPPGTGKTLLAKATAGE--SAVPFLSISGSDF 396
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
331-496 1.79e-04

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: 44.84  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   331 GCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGA---LLVGPPGTGKTLLAKATA------GESAVPFL-SISGSDFMEMF 400
Cdd:TIGR03922 280 GLERVKRQVAALKSSTAMALARAERGLPVAQTSnhmLFAGPPGTGKTTIARVVAkiycglGVLRKPLVrEVSRADLIGQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   401 VGVGPSRVRNLFQEArqcAPSIIFIDEIDAIgRARGRGgfsGGNDERESTLNQLLVEM----DGFgttagVVVLAGTNrp 476
Cdd:TIGR03922 360 IGESEAKTNEIIDSA---LGGVLFLDEAYTL-VETGYG---QKDPFGLEAIDTLLARMendrDRL-----VVIGAGYR-- 425
                         170       180
                  ....*....|....*....|....*
gi 22329400   477 DILDKAL-----LRpGRFDRQITID 496
Cdd:TIGR03922 426 KDLDKFLevnegLR-SRFTRVIEFP 449
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
364-434 1.96e-04

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 44.00  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 364 LLVGPPGTGKTLLAKATAGESAVPFL----------------SISGSDFMEMFVGVGPsrvrnLFQearqcapSIIFIDE 427
Cdd:COG0714  35 LLEGVPGVGKTTLAKALARALGLPFIriqftpdllpsdilgtYIYDQQTGEFEFRPGP-----LFA-------NVLLADE 102

                ....*..
gi 22329400 428 IDaigRA 434
Cdd:COG0714 103 IN---RA 106
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
364-434 3.93e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.58  E-value: 3.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329400  364 LLVGPPGTGKTLLAKATAGESAVPFLSISG------SDFMEMFVGVGPSrvrnlfqearqcapSIIFIDEIDAIGRA 434
Cdd:PRK00080  55 LLYGPPGLGKTTLANIIANEMGVNIRITSGpalekpGDLAAILTNLEEG--------------DVLFIDEIHRLSPV 117
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
364-433 3.97e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 43.61  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400  364 LLVGPPGTGKTLLAKATAGESAVPF-------LSISGsdfmemFVGvgpSRVRNLFQEARQCAP--------SIIFIDEI 428
Cdd:PRK05342 112 LLIGPTGSGKTLLAQTLARILDVPFaiadattLTEAG------YVG---EDVENILLKLLQAADydvekaqrGIVYIDEI 182

                 ....*
gi 22329400  429 DAIGR 433
Cdd:PRK05342 183 DKIAR 187
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
326-434 6.90e-04

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


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 42.67  E-value: 6.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   326 FKDVAGCEEAKQEIMEFVHflqnpkkyedlGAKIPKGA----LLVGPPGTGKTLLAKATAGESAVPFLSISG------SD 395
Cdd:TIGR00635   3 LAEFIGQEKVKEQLQLFIE-----------AAKMRQEAldhlLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGD 71
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 22329400   396 FMEMFVGVGPSrvrnlfqearqcapSIIFIDEIDAIGRA 434
Cdd:TIGR00635  72 LAAILTNLEEG--------------DVLFIDEIHRLSPA 96
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
358-434 2.06e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 41.11  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400 358 KIPKGALLVGPPGTGKTLLAKATA----GESAVP-----------FLSISGSDFMEMFVGVGPS-----RVRNLFQEARQ 417
Cdd:COG0470  16 RLPHALLLHGPPGIGKTTLALALArdllCENPEGgkacgqchsrlMAAGNHPDLLELNPEEKSDqigidQIRELGEFLSL 95
                        90       100
                ....*....|....*....|.
gi 22329400 418 CAPS----IIFIDEIDAIGRA 434
Cdd:COG0470  96 TPLEggrkVVIIDEADAMNEA 116
44 PHA02544
clamp loader, small subunit; Provisional
358-434 2.63e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 40.74  E-value: 2.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329400  358 KIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVgvgPSRVRNLFQEARQCA-PSIIFIDEIDAIGRA 434
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSDCRIDFV---RNRLTRFASTVSLTGgGKVIIIDEFDRLGLA 115
AAA_22 pfam13401
AAA domain;
364-481 2.76e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329400   364 LLVGPPGTGKTLLAK---ATAGESAVPFLSI------SGSDFMEMFV---------GVGPSRVRNLFQEA--RQCAPSII 423
Cdd:pfam13401   9 VLTGESGTGKTTLLRrllEQLPEVRDSVVFVdlpsgtSPKDLLRALLralglplsgRLSKEELLAALQQLllALAVAVVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329400   424 FIDEIDAIgrargrggfsggndeRESTLNqLLVEMDGFGTTAGVVVLAGTnrPDILDK 481
Cdd:pfam13401  89 IIDEAQHL---------------SLEALE-ELRDLLNLSSKLLQLILVGT--PELREL 128
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
364-378 7.50e-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: 39.64  E-value: 7.50e-03
                        10
                ....*....|....*
gi 22329400 364 LLVGPPGTGKTLLAK 378
Cdd:COG0606 215 LMIGPPGSGKTMLAR 229
PRK13341 PRK13341
AAA family ATPase;
363-428 8.65e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.65  E-value: 8.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22329400  363 ALLVGPPGTGKTLLAKATAGESAVPFLSISGsdfmemfVGVGPSRVRNLFQEARQ-----CAPSIIFIDEI 428
Cdd:PRK13341  55 LILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKErlerhGKRTILFIDEV 118
 
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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