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Conserved domains on  [gi|14090194|emb|CAC13952|]
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CELL DIVISION PROTEIN FTSH [Mycoplasmopsis pulmonis]

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];
20-650 0e+00

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


:

Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 723.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  20 IAALLITVLVLLFSPKTQPKSFDYllKHFEEAAKSttDDIyfETIKINslDNTIGVIFRNGamREEYFVAASAAQANFLt 99
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSVKEISY--SEFLQLVEA--GKV--KSVTIQ--GDRITGTLKDG--TKTRFTTYRVNDPELV- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 100 sgnvevrEILQLANVQayiqsiktlngtiswftfmnkflaqhpgydaskaglFGQHIVQENGFITFIKAIWFPALIAIII 179
Cdd:COG0465  70 -------DLLEEKGVE------------------------------------VTAKPPEESSWLLSLLISLLPILLLIGL 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 180 FLGYKAQSRAASGGIFNPGKNQA-VIVKTDKK--FTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGT 256
Cdd:COG0465 107 WIFFMRRMQGGGGGAMSFGKSKAkLYDEDKPKvtFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGT 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 257 GKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLN 336
Cdd:COG0465 187 GKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLN 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 337 QILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGY 416
Cdd:COG0465 267 QLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGF 346
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 417 SGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAYHEAGHAVVGLKVKGGNKVQKITI 496
Cdd:COG0465 347 SGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTI 426
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 497 IPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKenISTGASDDISRATKIARKMVTEWGMS-ALGPI 575
Cdd:COG0465 427 IPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSeKLGPV 504
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194 576 KYEEDTENPFLGRDYSKG-TFGSKMAHEIDLEIRKIISASEEIAIKAIEQNLELLELIKDSLLENETIVAEEIEYI 650
Cdd:COG0465 505 AYGESEGEVFLGRDIGQSrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEI 580
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
20-650 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 723.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  20 IAALLITVLVLLFSPKTQPKSFDYllKHFEEAAKSttDDIyfETIKINslDNTIGVIFRNGamREEYFVAASAAQANFLt 99
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSVKEISY--SEFLQLVEA--GKV--KSVTIQ--GDRITGTLKDG--TKTRFTTYRVNDPELV- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 100 sgnvevrEILQLANVQayiqsiktlngtiswftfmnkflaqhpgydaskaglFGQHIVQENGFITFIKAIWFPALIAIII 179
Cdd:COG0465  70 -------DLLEEKGVE------------------------------------VTAKPPEESSWLLSLLISLLPILLLIGL 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 180 FLGYKAQSRAASGGIFNPGKNQA-VIVKTDKK--FTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGT 256
Cdd:COG0465 107 WIFFMRRMQGGGGGAMSFGKSKAkLYDEDKPKvtFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGT 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 257 GKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLN 336
Cdd:COG0465 187 GKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLN 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 337 QILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGY 416
Cdd:COG0465 267 QLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGF 346
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 417 SGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAYHEAGHAVVGLKVKGGNKVQKITI 496
Cdd:COG0465 347 SGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTI 426
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 497 IPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKenISTGASDDISRATKIARKMVTEWGMS-ALGPI 575
Cdd:COG0465 427 IPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSeKLGPV 504
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194 576 KYEEDTENPFLGRDYSKG-TFGSKMAHEIDLEIRKIISASEEIAIKAIEQNLELLELIKDSLLENETIVAEEIEYI 650
Cdd:COG0465 505 AYGESEGEVFLGRDIGQSrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEI 580
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
170-650 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: 660.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   170 WFPA-LIAIIIFLGYKAQSRAASGGIFNPGKNQAVIVKTDK---KFTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFP 245
Cdd:TIGR01241   9 LLPPiLLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKpkvTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   246 KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIG 325
Cdd:TIGR01241  89 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   326 GGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIK 405
Cdd:TIGR01241 169 GGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   406 FDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAYHEAGHAVVGLKV 485
Cdd:TIGR01241 249 LKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   486 KGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGkeNISTGASDDISRATKIARKMVT 565
Cdd:TIGR01241 329 KDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   566 EWGMS-ALGPIKYEEDTENPFLGRDYSKGT-FGSKMAHEIDLEIRKIISASEEIAIKAIEQNLELLELIKDSLLENETIV 643
Cdd:TIGR01241 407 EWGMSdKLGPVAYGSDGGDVFLGRGFAKAKeYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETIT 486

                  ....*..
gi 14090194   644 AEEIEYI 650
Cdd:TIGR01241 487 REEIKEL 493
ftsH CHL00176
cell division protein; Validated
156-664 5.70e-171

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 504.97  E-value: 5.70e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  156 IVQENGFITFIKAIWFPALIAIIIFLGYKAQSRAASG---GIFNPGKNQAVI---VKTDKKFTDIAGNKEPIEEVQELVD 229
Cdd:CHL00176 121 PVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGpgqNLMNFGKSKARFqmeADTGITFRDIAGIEEAKEEFEEVVS 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  230 YLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIF 309
Cdd:CHL00176 201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  310 IDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREE 389
Cdd:CHL00176 281 IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLD 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  390 ILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEElK 469
Cdd:CHL00176 361 ILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNK-R 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  470 AVAYHEAGHAVVGLKVKGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKENISTGA 549
Cdd:CHL00176 440 LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGA 519
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  550 SDDISRATKIARKMVTEWGMSALGPIKYEED-TENPFLGRDYSKGTFGSK-MAHEIDLEIRKIISASEEIAIKAIEQNLE 627
Cdd:CHL00176 520 SNDLQQVTNLARQMVTRFGMSSIGPISLESNnSTDPFLGRFMQRNSEYSEeIADKIDMEVRSILHTCYQYAYQILKDNRV 599
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 14090194  628 LLELIKDSLLENETIVAEEI-EYIEKNMKLPPNNEKIK 664
Cdd:CHL00176 600 LIDLLVELLLQKETIDGDEFrEIVNSYTILPPKKTWKA 637
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
210-379 4.99e-97

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: 296.84  E-value: 4.99e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 210 KFTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:cd19501   2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLR 369
Cdd:cd19501  82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLR 161
                       170
                ....*....|
gi 14090194 370 PGRFDRIITV 379
Cdd:cd19501 162 PGRFDRQVYV 171
Peptidase_M41 pfam01434
Peptidase family M41;
461-650 5.81e-75

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 240.20  E-value: 5.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   461 RVISQEELKAVAYHEAGHAVVGLKVKGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIY 540
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   541 GKenISTGASDDISRATKIARKMVTEWGMS-ALGPIKYEEDTENPFLGRDYSKG-TFGSKMAHEIDLEIRKIISASEEIA 618
Cdd:pfam01434  81 GE--VTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEESDGNVFLGRGMGKRkPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 14090194   619 IKAIEQNLELLELIKDSLLENETIVAEEIEYI 650
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
245-383 1.37e-15

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: 74.33  E-value: 1.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194    245 PKGILLGGPPGTGKTLLAKATAGEANVP---FFFISASSFVE--------------LYVGLGAKRVREMFKEARKLAPAI 307
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194    308 IFIDELDAVGRSRGsgigggndEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPgRFDRIITVGLPD 383
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
248-313 3.86e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 3.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  248 ILLGGPPGTGKTLLAKAT---AGEANVPFFFISASSFVELYvgLGAKRVREMFKEARKLA-PAIIFIDEL 313
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRFTTAADLVEQL--AQARADGRLGRLLRRLArYDLLIIDEL 160
 
Name Accession Description Interval E-value
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
20-650 0e+00

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 723.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  20 IAALLITVLVLLFSPKTQPKSFDYllKHFEEAAKSttDDIyfETIKINslDNTIGVIFRNGamREEYFVAASAAQANFLt 99
Cdd:COG0465   1 IALLLVLLFNLFSSSSSSVKEISY--SEFLQLVEA--GKV--KSVTIQ--GDRITGTLKDG--TKTRFTTYRVNDPELV- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 100 sgnvevrEILQLANVQayiqsiktlngtiswftfmnkflaqhpgydaskaglFGQHIVQENGFITFIKAIWFPALIAIII 179
Cdd:COG0465  70 -------DLLEEKGVE------------------------------------VTAKPPEESSWLLSLLISLLPILLLIGL 106
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 180 FLGYKAQSRAASGGIFNPGKNQA-VIVKTDKK--FTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGT 256
Cdd:COG0465 107 WIFFMRRMQGGGGGAMSFGKSKAkLYDEDKPKvtFDDVAGVDEAKEELQEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGT 186
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 257 GKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLN 336
Cdd:COG0465 187 GKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLN 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 337 QILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGY 416
Cdd:COG0465 267 QLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGF 346
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 417 SGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAYHEAGHAVVGLKVKGGNKVQKITI 496
Cdd:COG0465 347 SGADLANLVNEAALLAARRNKKAVTMEDFEEAIDRVIAGPERKSRVISEKEKKITAYHEAGHALVAALLPGADPVHKVTI 426
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 497 IPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKenISTGASDDISRATKIARKMVTEWGMS-ALGPI 575
Cdd:COG0465 427 IPRGRALGYTMQLPEEDRYLYTKEELLDRIAVLLGGRAAEELVFGE--VTTGASNDLERATKIARAMVTEYGMSeKLGPV 504
                       570       580       590       600       610       620       630
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194 576 KYEEDTENPFLGRDYSKG-TFGSKMAHEIDLEIRKIISASEEIAIKAIEQNLELLELIKDSLLENETIVAEEIEYI 650
Cdd:COG0465 505 AYGESEGEVFLGRDIGQSrNYSEETAREIDEEVRRIIDEAYERAKEILTENRDKLDALAEALLEKETLDGEELEEI 580
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
170-650 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: 660.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   170 WFPA-LIAIIIFLGYKAQSRAASGGIFNPGKNQAVIVKTDK---KFTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFP 245
Cdd:TIGR01241   9 LLPPiLLLVGVWFFFRRQMQGGGGRAFSFGKSKAKLLNEEKpkvTFKDVAGIDEAKEELMEIVDFLKNPSKFTKLGAKIP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   246 KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIG 325
Cdd:TIGR01241  89 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   326 GGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIK 405
Cdd:TIGR01241 169 GGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVD 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   406 FDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAYHEAGHAVVGLKV 485
Cdd:TIGR01241 249 LKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAIDRVIAGPEKKSRVISEKEKKLVAYHEAGHALVGLLL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   486 KGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGkeNISTGASDDISRATKIARKMVT 565
Cdd:TIGR01241 329 KDADPVHKVTIIPRGQALGYTQFLPEEDKYLYTKSQLLAQIAVLLGGRAAEEIIFG--EVTTGASNDIKQATNIARAMVT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   566 EWGMS-ALGPIKYEEDTENPFLGRDYSKGT-FGSKMAHEIDLEIRKIISASEEIAIKAIEQNLELLELIKDSLLENETIV 643
Cdd:TIGR01241 407 EWGMSdKLGPVAYGSDGGDVFLGRGFAKAKeYSEETAREIDEEVKRIIEEAYKRAKQILTENRDELELLAKALLEKETIT 486

                  ....*..
gi 14090194   644 AEEIEYI 650
Cdd:TIGR01241 487 REEIKEL 493
ftsH CHL00176
cell division protein; Validated
156-664 5.70e-171

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 504.97  E-value: 5.70e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  156 IVQENGFITFIKAIWFPALIAIIIFLGYKAQSRAASG---GIFNPGKNQAVI---VKTDKKFTDIAGNKEPIEEVQELVD 229
Cdd:CHL00176 121 PVLKSNIVTILSNLLLPLILIGVLWFFFQRSSNFKGGpgqNLMNFGKSKARFqmeADTGITFRDIAGIEEAKEEFEEVVS 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  230 YLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIF 309
Cdd:CHL00176 201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVF 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  310 IDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREE 389
Cdd:CHL00176 281 IDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLD 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  390 ILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEElK 469
Cdd:CHL00176 361 ILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDTAIDRVIAGLEGTPLEDSKNK-R 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  470 AVAYHEAGHAVVGLKVKGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKENISTGA 549
Cdd:CHL00176 440 LIAYHEVGHAIVGTLLPNHDPVQKVTLIPRGQAKGLTWFTPEEDQSLVSRSQILARIVGALGGRAAEEVVFGSTEVTTGA 519
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  550 SDDISRATKIARKMVTEWGMSALGPIKYEED-TENPFLGRDYSKGTFGSK-MAHEIDLEIRKIISASEEIAIKAIEQNLE 627
Cdd:CHL00176 520 SNDLQQVTNLARQMVTRFGMSSIGPISLESNnSTDPFLGRFMQRNSEYSEeIADKIDMEVRSILHTCYQYAYQILKDNRV 599
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 14090194  628 LLELIKDSLLENETIVAEEI-EYIEKNMKLPPNNEKIK 664
Cdd:CHL00176 600 LIDLLVELLLQKETIDGDEFrEIVNSYTILPPKKTWKA 637
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
158-673 1.24e-161

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 481.07  E-value: 1.24e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  158 QENGFITFIKAIWFPALIAIIIFLGYKAQSRAASG-GIFNPGKNQAVIVKTDK---KFTDIAGNKEPIEEVQELVDYLKN 233
Cdd:PRK10733  94 EEPSLLASIFISWFPMLLLIGVWIFFMRQMQGGGGkGAMSFGKSKARMLTEDQiktTFADVAGCDEAKEEVAELVEYLRE 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  234 PKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDEL 313
Cdd:PRK10733 174 PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEI 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  314 DAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKL 393
Cdd:PRK10733 254 DAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKV 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  394 HSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEELKAVAY 473
Cdd:PRK10733 334 HMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSMVEFEKAKDKIMMGAERRSMVMTEAQKESTAY 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  474 HEAGHAVVGLKVKGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIYGKENISTGASDDI 553
Cdd:PRK10733 414 HEAGHAIIGRLVPEHDPVHKVTIIPRGRALGVTFFLPEGDAISASRQKLESQISTLYGGRLAEEIIYGPEHVSTGASNDI 493
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  554 SRATKIARKMVTEWGMS-ALGPIKYEEDTENPFLGRDYSKGTFGS-KMAHEIDLEIRKIISASEEIAIKAIEQNLELLEL 631
Cdd:PRK10733 494 KVATNLARNMVTQWGFSeKLGPLLYAEEEGEVFLGRSVAKAKHMSdETARIIDQEVKALIERNYNRARQLLTDNMDILHA 573
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 14090194  632 IKDSLLENETIVAEEIEYIEKNMKLPPNNEKIKPDGESKKVN 673
Cdd:PRK10733 574 MKDALMKYETIDAPQIDDLMARRDVRPPAGWEEPGASNNSDD 615
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
210-379 4.99e-97

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: 296.84  E-value: 4.99e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 210 KFTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:cd19501   2 TFKDVAGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLR 369
Cdd:cd19501  82 ASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLR 161
                       170
                ....*....|
gi 14090194 370 PGRFDRIITV 379
Cdd:cd19501 162 PGRFDRQVYV 171
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
206-461 1.24e-94

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 296.53  E-value: 1.24e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 206 KTDKKFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVEL 284
Cdd:COG1222  72 SPDVTFDDIGGLDEQIEEIREAVELpLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 285 YVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGggNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLD 364
Cdd:COG1222 152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGT--SGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLD 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 365 PALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQ 444
Cdd:COG1222 230 PALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVTMED 309
                       250
                ....*....|....*..
gi 14090194 445 IDEAIDRVMAGPAKKSR 461
Cdd:COG1222 310 LEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
203-460 6.64e-84

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 270.94  E-value: 6.64e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  203 VIVKTDKKFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSF 281
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELpLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  282 VELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTD 361
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAEMDGFDPRGNVKIIAATNRID 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  362 VLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVII 441
Cdd:PRK03992 282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRTEVT 361
                        250
                 ....*....|....*....
gi 14090194  442 STQIDEAIDRVMAGPAKKS 460
Cdd:PRK03992 362 MEDFLKAIEKVMGKEEKDS 380
Peptidase_M41 pfam01434
Peptidase family M41;
461-650 5.81e-75

Peptidase family M41;


Pssm-ID: 460210 [Multi-domain]  Cd Length: 190  Bit Score: 240.20  E-value: 5.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   461 RVISQEELKAVAYHEAGHAVVGLKVKGGNKVQKITIIPRGNAGGYNLMTPEEEKYNASKKELLATIASYMGGRAAEMIIY 540
Cdd:pfam01434   1 RVISEEEKKIVAYHEAGHALVGLLLPGADPVHKVTIIPRGQALGYTQFLPEEDKLLYTKEQLLARIAVLLGGRAAEELIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   541 GKenISTGASDDISRATKIARKMVTEWGMS-ALGPIKYEEDTENPFLGRDYSKG-TFGSKMAHEIDLEIRKIISASEEIA 618
Cdd:pfam01434  81 GE--VTTGASNDLEKATKIARQMVTEFGMSdKLGPVSLEESDGNVFLGRGMGKRkPYSEETADIIDEEVKRLLEEAYERA 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 14090194   619 IKAIEQNLELLELIKDSLLENETIVAEEIEYI 650
Cdd:pfam01434 159 KEILTEHRDELEALAEALLEKETLDAEEIREL 190
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
203-453 4.52e-73

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: 241.24  E-value: 4.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   203 VIVKTDKKFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSF 281
Cdd:TIGR01242 113 VEERPNVSYEDIGGLEEQIREIREAVELpLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   282 VELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTD 361
Cdd:TIGR01242 193 VRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPD 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   362 VLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVII 441
Cdd:TIGR01242 273 ILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDYVT 352
                         250
                  ....*....|..
gi 14090194   442 STQIDEAIDRVM 453
Cdd:TIGR01242 353 MDDFIKAVEKVL 364
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
211-452 2.29e-68

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 229.80  E-value: 2.29e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 211 FTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALpLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVgrsrGSGIGGGNDEREQT-LNQILVEMDGINENagILIMGATNRTDVLDPALL 368
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADAL----AGKRGEVGDGVGRRvVNTLLTEMEELRSD--VVVIAATNRPDLLDPALL 309
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 369 RpgRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEA 448
Cdd:COG0464 310 R--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLLEA 387

                ....
gi 14090194 449 IDRV 452
Cdd:COG0464 388 LERE 391
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
210-471 4.74e-60

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: 215.54  E-value: 4.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   210 KFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGL 288
Cdd:TIGR01243 451 RWSDIGGLEEVKQELREAVEWpLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGE 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   289 GAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEReqTLNQILVEMDGINENAGILIMGATNRTDVLDPALL 368
Cdd:TIGR01243 531 SEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR--IVNQLLTEMDGIQELSNVVVIAATNRPDILDPALL 608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   369 RPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREktdvIISTQIDEA 448
Cdd:TIGR01243 609 RPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRE----SIGSPAKEK 684
                         250       260
                  ....*....|....*....|...
gi 14090194   449 IDRVMAGPAKKSRVISQEELKAV 471
Cdd:TIGR01243 685 LEVGEEEFLKDLKVEMRHFLEAL 707
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
211-379 2.21e-55

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 187.16  E-value: 2.21e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 211 FTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLR 369
Cdd:cd19502  82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                       170
                ....*....|
gi 14090194 370 PGRFDRIITV 379
Cdd:cd19502 162 PGRFDRKIEF 171
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
211-451 5.32e-55

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 188.94  E-value: 5.32e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 211 FTDIAGNKEPIEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGA 290
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 291 KRVREMFKEARKlAPAIIFIDELDAVgrsrGSGIGGGNDERE--QTLNQILVEMDGINEnaGILIMGATNRTDVLDPALL 368
Cdd:COG1223  81 RNLRKLFDFARR-APCVIFFDEFDAI----AKDRGDQNDVGEvkRVVNALLQELDGLPS--GSVVIAATNHPELLDSALW 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 369 RpgRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDEA 448
Cdd:COG1223 154 R--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEEA 231

                ...
gi 14090194 449 IDR 451
Cdd:COG1223 232 LKQ 234
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
221-379 1.99e-54

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 184.02  E-value: 1.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 221 IEEVQELVDYLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEA 300
Cdd:cd19481   2 KASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 301 RKLAPAIIFIDELDAVgrSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19481  82 RRLAPCILFIDEIDAI--GRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
199-434 1.67e-52

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: 194.36  E-value: 1.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   199 KNQAVIVKTDKK-----FTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVP 272
Cdd:TIGR01243 160 REKPVREEIERKvpkvtYEDIGGLKEAKEKIREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   273 FFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGINENAGIL 352
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAI---APKREEVTGEVEKRVVAQLLTLMDGLKGRGRVI 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   353 IMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLS 432
Cdd:TIGR01243 317 VIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAA 396

                  ..
gi 14090194   433 VR 434
Cdd:TIGR01243 397 LR 398
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
222-379 1.89e-52

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: 178.63  E-value: 1.89e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 222 EEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEA 300
Cdd:cd19511   3 RELKEAVEWpLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 301 RKLAPAIIFIDELDAVGRSRGSGIGGGNDEReqTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19511  83 RQAAPCIIFFDEIDSLAPRRGQSDSSGVTDR--VVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
213-377 1.48e-50

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: 173.63  E-value: 1.48e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAK 291
Cdd:cd19503   1 DIGGLDEQIASLKELIELpLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 292 RVREMFKEARKLAPAIIFIDELDAVgrsrgsGIGGGNDEREQ---TLNQILVEMDGINENAGILIMGATNRTDVLDPALL 368
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDAL------APKREEDQREVerrVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALR 154

                ....*....
gi 14090194 369 RPGRFDRII 377
Cdd:cd19503 155 RPGRFDREV 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
206-453 8.47e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 176.88  E-value: 8.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  206 KTDKKFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVEL 284
Cdd:PTZ00454 139 KPDVTYSDIGGLDIQKQEIREAVELpLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQK 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  285 YVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLD 364
Cdd:PTZ00454 219 YLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLD 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  365 PALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQ 444
Cdd:PTZ00454 299 PALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRKNRYVILPKD 378

                 ....*....
gi 14090194  445 IDEAIDRVM 453
Cdd:PTZ00454 379 FEKGYKTVV 387
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
204-436 6.82e-48

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 175.34  E-value: 6.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  204 IVKTDK----KFTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISA 278
Cdd:PTZ00361 171 VMKVDKapleSYADIGGLEQQIQEIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVG 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  279 SSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATN 358
Cdd:PTZ00361 251 SELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELLNQLDGFDSRGDVKVIMATN 330
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14090194  359 RTDVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFDKIAKRTPGYSGAQLENVINEASLLSVREK 436
Cdd:PTZ00361 331 RIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRER 408
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
222-379 1.45e-47

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: 165.36  E-value: 1.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 222 EEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEA 300
Cdd:cd19529   3 QELKEAVEWpLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 301 RKLAPAIIFIDELDAVGRSRGSGIGGGNDEReqTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19529  83 RQVAPCVIFFDEIDSIAPRRGTTGDSGVTER--VVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
248-381 4.43e-45

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 157.37  E-value: 4.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   248 ILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGG 327
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL---AGSRGSGG 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 14090194   328 NDEREQTLNQILVEMDGI-NENAGILIMGATNRTDVLDPALLrpGRFDRIITVGL 381
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
222-379 4.38e-44

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: 155.75  E-value: 4.38e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 222 EEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEA 300
Cdd:cd19528   3 RELQELVQYpVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 301 RKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19528  83 RAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
213-380 1.28e-42

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: 151.82  E-value: 1.28e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAK 291
Cdd:cd19519   1 DIGGCRKQLAQIREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 292 RVREMFKEARKLAPAIIFIDELDAVgrsrGSGIGGGNDEREQTL-NQILVEMDGINENAGILIMGATNRTDVLDPALLRP 370
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAI----APKREKTHGEVERRIvSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156
                       170
                ....*....|
gi 14090194 371 GRFDRIITVG 380
Cdd:cd19519 157 GRFDREIDIG 166
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
213-377 1.59e-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: 1.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVDYLKNPKKYAAA-GARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAK 291
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHlGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 292 RVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGINEN----AGILIMGATNRTDVLDPAL 367
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAI---TPKRESAQREMERRIVSQLLTCMDELNNEktagGPVLVIGATNRPDSLDPAL 157
                       170
                ....*....|
gi 14090194 368 LRPGRFDRII 377
Cdd:cd19518 158 RRAGRFDREI 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
231-379 2.93e-42

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: 150.72  E-value: 2.93e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 231 LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFI 310
Cdd:cd19530  16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIFF 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 311 DELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19530  96 DEVDAL---VPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
218-377 9.98e-37

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 135.25  E-value: 9.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 218 KEPIEEVQELVDylKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMF 297
Cdd:cd19526   2 KKALEETIEWPS--KYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 298 KEARKLAPAIIFIDELDAVGRSRGSGIGGGNDereQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPGRFDRII 377
Cdd:cd19526  80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTD---RVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
214-379 3.20e-36

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: 134.02  E-value: 3.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 214 IAGNKEPIEEVQELVDY-LKNPKKYAAaGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKR 292
Cdd:cd19509   1 IAGLDDAKEALKEAVILpSLRPDLFPG-LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 293 VREMFKEARKLAPAIIFIDELDAVGRSRGSGIGggndEREQTL-NQILVEMDGI--NENAGILIMGATNRTDVLDPALLR 369
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEH----EASRRVkTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR 155
                       170
                ....*....|
gi 14090194 370 pgRFDRIITV 379
Cdd:cd19509 156 --RFEKRIYI 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
226-379 5.39e-35

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: 130.33  E-value: 5.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 226 ELVDYLKNPKKYA---AAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARK 302
Cdd:cd19527   4 EILDTIQLPLEHPelfSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14090194 303 LAPAIIFIDELDAVgRSRGSGIGGGNDEREQTLNQILVEMDGINENA-GILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19527  84 AKPCVIFFDELDSL-APSRGNSGDSGGVMDRVVSQLLAELDGMSSSGqDVFVIGATNRPDLLDPALLRPGRFDKLLYL 160
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
213-379 2.92e-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: 122.65  E-value: 2.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVdYLKNPKKYAAAGARFP-KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAK 291
Cdd:cd19524   1 DIAGQDLAKQALQEMV-ILPSLRPELFTGLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 292 RVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGINENAG--ILIMGATNRTDVLDPALLR 369
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSL---LSERSEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
                       170
                ....*....|
gi 14090194 370 pgRFDRIITV 379
Cdd:cd19524 157 --RFTKRVYV 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
213-375 1.57e-31

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: 120.69  E-value: 1.57e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVDY-LKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEAN-----VPFFFISASSFVELYV 286
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFpLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 287 GLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRgsgigggNDEREQTLNQI----LVEMDGINENAGILIMGATNRTDV 362
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVR-------SSKQEQIHASIvstlLALMDGLDNRGQVVVIGATNRPDA 153
                       170
                ....*....|...
gi 14090194 363 LDPALLRPGRFDR 375
Cdd:cd19517 154 LDPALRRPGRFDR 166
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
206-379 4.13e-30

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: 116.89  E-value: 4.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 206 KTDKKFTDIAGNKEPIEEVQELVDY-LKNPKKYAaaGARFP-KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVE 283
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILpVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 284 LYVGLGAKRVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGI-NENAGILIMGATNRTDV 362
Cdd:cd19521  79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSL---CGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQ 155
                       170
                ....*....|....*..
gi 14090194 363 LDPALLRpgRFDRIITV 379
Cdd:cd19521 156 LDSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
213-373 6.52e-29

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: 113.29  E-value: 6.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELVDY-LKNPKKYAAAG-ARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGA 290
Cdd:cd19520   1 DIGGLDEVITELKELVILpLQRPELFDNSRlLQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 291 KRVREMFKEARKLAPAIIFIDELDAVGRSRGSGigggndEREQTL---NQILVEMDGI--NENAGILIMGATNRTDVLDP 365
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST------DHEATAmmkAEFMSLWDGLstDGNCRVIVMGATNRPQDLDE 154
                       170
                ....*....|
gi 14090194 366 ALLR--PGRF 373
Cdd:cd19520 155 AILRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
211-369 1.04e-26

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: 107.77  E-value: 1.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 211 FTDIAGNKEPIEEVQELVDY-LKNPKKYAAAGARfPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:cd19525  21 WADIAGLEFAKKTIKEIVVWpMLRPDIFTGLRGP-PKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVgrsRGSGIGGGNDEREQTLNQILVEMDGINENAG--ILIMGATNRTDVLDPAL 367
Cdd:cd19525 100 EKMVRALFSVARCKQPAVIFIDEIDSL---LSQRGEGEHESSRRIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAA 176

                ..
gi 14090194 368 LR 369
Cdd:cd19525 177 RR 178
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
213-369 3.72e-24

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: 99.67  E-value: 3.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGNKEPIEEVQELV-------DYLKnpkkyaaaGARFP-KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVEL 284
Cdd:cd19522   1 DIADLEEAKKLLEEAVvlpmwmpEFFK--------GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 285 YVGLGAKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNDEREQTlnQILVEMDGIN---ENAG----ILIMGAT 357
Cdd:cd19522  73 YRGESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKS--ELLVQMDGVGgasENDDpskmVMVLAAT 150
                       170
                ....*....|..
gi 14090194 358 NRTDVLDPALLR 369
Cdd:cd19522 151 NFPWDIDEALRR 162
ycf46 CHL00195
Ycf46; Provisional
207-444 2.46e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 104.33  E-value: 2.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  207 TDKKFTDIAGnkepieeVQELVDYLKN-----PKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSF 281
Cdd:CHL00195 223 VNEKISDIGG-------LDNLKDWLKKrstsfSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  282 VELYVGLGAKRVREMFKEARKLAPAIIFIDELD-AVGRSRGSGIGGGNDEREQTLNQILVEmdginENAGILIMGATNRT 360
Cdd:CHL00195 296 FGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLSE-----KKSPVFVVATANNI 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  361 DVLDPALLRPGRFDRIITVGLPDIKEREEILKLHSKGKRLSKEIKFD--KIAKRTPGYSGAQLENVINEASLLSVREK-- 436
Cdd:CHL00195 371 DLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYDikKLSKLSNKFSGAEIEQSIIEAMYIAFYEKre 450
                        250
                 ....*....|.
gi 14090194  437 ---TDVIISTQ 444
Cdd:CHL00195 451 fttDDILLALK 461
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
218-381 2.60e-22

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: 93.75  E-value: 2.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 218 KEPIEEVQELVDYLKNPKkyaaagarfPKGILLGGPPGTGKTLLAKATAGEA---NVPFFFISASSFVELYVGLGAKR-- 292
Cdd:cd00009   1 VGQEEAIEALREALELPP---------PKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhf 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 293 -VREMFKEARKLAPAIIFIDELDAVgrsrgsgiggGNDEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPG 371
Cdd:cd00009  72 lVRLLFELAEKAKPGVLFIDEIDSL----------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYD 141
                       170
                ....*....|
gi 14090194 372 RFDRIITVGL 381
Cdd:cd00009 142 RLDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
208-374 1.08e-21

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: 92.94  E-value: 1.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 208 DKKFTDI-----AGNKEPIEEVQELvdylknpkkyaaaGARFPKGILLGGPPGTGKTLLAKA-----TAGEANVpfffIS 277
Cdd:cd19504   6 DKEFSDIfrrafASRVFPPEIVEQL-------------GCKHVKGILLYGPPGTGKTLMARQigkmlNAREPKI----VN 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 278 ASSFVELYVGLGAKRVREMFKEA----RKLAPA----IIFIDELDAVGRSRGSGIGGGNdEREQTLNQILVEMDGINENA 349
Cdd:cd19504  69 GPEILNKYVGESEANIRKLFADAeeeqRRLGANsglhIIIFDEIDAICKQRGSMAGSTG-VHDTVVNQLLSKIDGVEQLN 147
                       170       180
                ....*....|....*....|....*
gi 14090194 350 GILIMGATNRTDVLDPALLRPGRFD 374
Cdd:cd19504 148 NILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
235-379 3.06e-18

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: 82.42  E-value: 3.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 235 KKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKRVREMFKEARKLAPAIIFIDELD 314
Cdd:cd19507  21 KQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIE 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14090194 315 AVGRSRGSGIGGGNDEReqTLNQILVEMDgiNENAGILIMGATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19507 101 KGFSNADSKGDSGTSSR--VLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
224-379 1.90e-17

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 79.70  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 224 VQELVDYLKNPKKYAAAGARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSfvelyVGLGAKRVREMFKEARKl 303
Cdd:cd19510   2 IDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSE-----VVLTDDRLNHLLNTAPK- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 304 aPAIIFIDELDAV---GRSRGSGIGGGNDEREQTLNQILVEMDGI-NENAGILIMgATNRTDVLDPALLRPGRFDRIITV 379
Cdd:cd19510  76 -QSIILLEDIDAAfesREHNKKNPSAYGGLSRVTFSGLLNALDGVaSSEERIVFM-TTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
213-369 3.10e-17

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: 79.54  E-value: 3.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 213 DIAGN---KEPIEEvqELVDYLKNPKKYAAAgARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLG 289
Cdd:cd19523   1 DIAGLgalKAAIKE--EVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 290 AKRVREMFKEARKLAPAIIFIDELDAVGRSRGSGIGGGNdeREQTlnQILVEMDGINENA--GILIMGATNRTDVLDPAL 367
Cdd:cd19523  78 EKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG--RLQV--ELLAQLDGVLGSGedGVLVVCTTSKPEEIDESL 153

                ..
gi 14090194 368 LR 369
Cdd:cd19523 154 RR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
245-383 1.37e-15

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: 74.33  E-value: 1.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194    245 PKGILLGGPPGTGKTLLAKATAGEANVP---FFFISASSFVE--------------LYVGLGAKRVREMFKEARKLAPAI 307
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194    308 IFIDELDAVGRSRGsgigggndEREQTLNQILVEMDGINENAGILIMGATNRTDVLDPALLRPgRFDRIITVGLPD 383
Cdd:smart00382  82 LILDEITSLLDAEQ--------EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
248-312 7.17e-10

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 61.64  E-value: 7.17e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194  248 ILLGGPPGTGKTLLAKATAGEANVPFFFISASSFvelyvglGAKRVREMFKEARKLAPA----IIFIDE 312
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVTS-------GVKDLREVIEEARQRRSAgrrtILFIDE 100
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
220-316 6.97e-09

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: 55.85  E-value: 6.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 220 PIEEVQELVDYL---KNPKKYAAAGAR----------------FPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASS 280
Cdd:cd19498   2 PREIVSELDKYIigqDEAKRAVAIALRnrwrrmqlpeelrdevTPKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATK 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 14090194 281 FVEL-YVGlgaKRVREMFkeaRKLAPAIIFIDELDAV 316
Cdd:cd19498  82 FTEVgYVG---RDVESII---RDLVEGIVFIDEIDKI 112
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
248-312 7.21e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 58.53  E-value: 7.21e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPFFFISAssfvelyVGLGAKRVREMFKEARKLA----PAIIFIDE 312
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDE 113
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
403-447 1.08e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 51.39  E-value: 1.08e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 14090194   403 EIKFDKIAKRTPGYSGAQLENVINEASLLSVREKTDVIISTQIDE 447
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
241-379 3.20e-08

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: 53.53  E-value: 3.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 241 GARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFV--------------ELYVGLGAKRVREMFKEARKLAPA 306
Cdd:cd19505   8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLynkpdfgnddwidgMLILKESLHRLNLQFELAKAMSPC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 307 IIF---IDELDAVGRSRGSGIGGG------------NDEREQTLNqilvemdginenagILIMGATNRTDVLDPALLRPG 371
Cdd:cd19505  88 IIWipnIHELNVNRSTQNLEEDPKlllglllnylsrDFEKSSTRN--------------ILVIASTHIPQKVDPALIAPN 153

                ....*...
gi 14090194 372 RFDRIITV 379
Cdd:cd19505 154 RLDTCINI 161
PRK04195 PRK04195
replication factor C large subunit; Provisional
209-314 1.79e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 54.16  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  209 KKFTDIAGNKEPIEEVQELVD-YLKNPKKyaaagarfpKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSF-----V 282
Cdd:PRK04195  11 KTLSDVVGNEKAKEQLREWIEsWLKGKPK---------KALLLYGPPGVGKTSLAHALANDYGWEVIELNASDQrtadvI 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 14090194  283 ELYVGLGAKRvREMFKEARKLapaiIFIDELD 314
Cdd:PRK04195  82 ERVAGEAATS-GSLFGARRKL----ILLDEVD 108
ycf2 CHL00206
Ycf2; Provisional
241-480 4.50e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 50.29  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   241 GARFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFV--------------------------------ELYVGL 288
Cdd:CHL00206 1626 ALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVFLNKFLdnkpkgfliddididdsddiddsddidrdldtELLTMM 1705
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   289 GAKRVREM-----------FKEARKLAPAIIFID---ELDAvgrsrgsgigggNDEREQTLNQILVEMDGINENAG---I 351
Cdd:CHL00206 1706 NALTMDMMpkidrfyitlqFELAKAMSPCIIWIPnihDLNV------------NESNYLSLGLLVNSLSRDCERCStrnI 1773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   352 LIMGATNRTDVLDPALLRPGRFDRIITVGLPDIKEREE---ILkLHSKGKRLSKEI----KFDKIakrTPGYSGAQLENV 424
Cdd:CHL00206 1774 LVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKhffTL-SYTRGFHLEKKMfhtnGFGSI---TMGSNARDLVAL 1849
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194   425 INEASLLSVREKTDVIISTQIDEAIDRVMAGPAKKSRVISQEElkaVAYHEAGHAV 480
Cdd:CHL00206 1850 TNEALSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQDHG---ILFYQIGRAV 1902
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
247-373 1.44e-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: 45.36  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   247 GILLGGPPGTGKTLLAKATAgEA--NVPFFFISASSF---------VELYVGLGAKRVREMFKEARKlaPAIIFIDELDa 315
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLA-AAlsNRPVFYVQLTRDtteedlfgrRNIDPGGASWVDGPLVRAARE--GEIAVLDEIN- 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14090194   316 vgrsrgsgigGGNDEREQTLNQILVE-----MDGINE----NAGILIMGATNRTD----VLDPALLRpgRF 373
Cdd:pfam07728  77 ----------RANPDVLNSLLSLLDErrlllPDGGELvkaaPDGFRLIATMNPLDrglnELSPALRS--RF 135
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
248-367 7.07e-05

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: 44.36  E-value: 7.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPFFF---------ISASSFVELYVGLGAKRVREMFKEARKLAP---AIIF--IDEL 313
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKLSIRLSSryrygqlieINSHSLFSKWFSESGKLVTKMFQKIQELIDdkdALVFvlIDEV 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194 314 DAVgRSRGSGIGGGNDERE--QTLNQILVEMDGINENAGILIMGATNRTDVLDPAL 367
Cdd:cd19508 135 ESL-AAARSASSSGTEPSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
246-285 1.01e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 45.35  E-value: 1.01e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 14090194 246 KGILLGGPPGTGKTLLAKATAGE--ANVPFFFISASsfvELY 285
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARElgEDTPFVAISGS---EIY 103
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
246-359 1.12e-04

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 43.29  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 246 KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGLGAKR--VREMFKEARKLAPAIIFIDELDAVGRSRGSG 323
Cdd:cd19506  27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNGLQmmLHLVLKVARQLQPSVIWIGDAEKTFYKKVPK 106
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 14090194 324 IGGGNDER--EQTLNQILVEMDGINEnagILIMGATNR 359
Cdd:cd19506 107 TEKQLDPKrlKKDLPKILKSLKPEDR---VLIVGTTSR 141
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
222-364 1.61e-04

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 44.45  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 222 EEVQELVDYLKnPkkyAAAGARfPKGILLGGPPGTGKTLLAKA-------TAGEANVPFFFI-----SASS----FVELY 285
Cdd:COG1474  33 EEIEELASALR-P---ALRGER-PSNVLIYGPTGTGKTAVAKYvleeleeEAEERGVDVRVVyvncrQASTryrvLSRIL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 286 -----------VGLGAKRVREMFKEA--RKLAPAIIFIDELDAVgrsrgsgiggGNDEREQTLNQiLVEMDGINENAGIL 352
Cdd:COG1474 108 eelgsgedipsTGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----------VDDEGDDLLYQ-LLRANEELEGARVG 176
                       170
                ....*....|..
gi 14090194 353 IMGATNRTDVLD 364
Cdd:COG1474 177 VIGISNDLEFLE 188
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
246-377 1.77e-04

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: 42.51  E-value: 1.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 246 KGILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVELYVGlGAKRVREMFKEARKLAPA-IIFIDELDAVgrSRGSGI 324
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAIHKVFDWANTSRRGlLLFVDEADAF--LRKRST 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 14090194 325 GGGNDEREQTLNQILVEMdGINENAGILIMgATNRTDVLDPALlrPGRFDRII 377
Cdd:cd19512 100 EKISEDLRAALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
246-285 2.40e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 43.84  E-value: 2.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 14090194   246 KGILLGGPPGTGKTLLAKATAGE--ANVPFFFISASsfvELY 285
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGS---EVY 89
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
248-314 2.78e-04

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: 43.36  E-value: 2.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVEL-YVGLGAKRVREMFKEA-----RKLAPAIIFIDELD 314
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAgYVGEDVENILLKLLQAadydvERAQRGIVYIDEID 125
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
246-313 2.78e-04

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 43.23  E-value: 2.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14090194 246 KGILLGGPPGTGKTLLAKA---TAGEANVPFFFISASSFV-ELYVGLGAKRVREMFKEARKlAPAIIfIDEL 313
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIAlghEACRAGYRVRFTTAPDLVnELKEARADGRLERLLKRLAK-VDLLI-LDEL 169
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
248-287 7.77e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 42.45  E-value: 7.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 14090194  248 ILLGGPPGTGKTLLAKATAGEANVPFFFISASSFVEL-YVG 287
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARILDVPFAIADATTLTEAgYVG 151
AAA_22 pfam13401
AAA domain;
242-363 1.12e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.63  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194   242 ARFPKGIL-LGGPPGTGKTLLAK---ATAGEANVPFFFISASSF---------------VELYVGLGAKRVREMFKEA-- 300
Cdd:pfam13401   1 IRFGAGILvLTGESGTGKTTLLRrllEQLPEVRDSVVFVDLPSGtspkdllrallralgLPLSGRLSKEELLAALQQLll 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14090194   301 RKLAPAIIFIDELDAVgrsrgsgigggndeREQTLNQILVEMDGINENAGILIMGATNRTDVL 363
Cdd:pfam13401  81 ALAVAVVLIIDEAQHL--------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
225-405 1.88e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.71  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 225 QELVDYLKNPKKYAAAGARFPKGILLGGPpGTGKT---------LLAKATAGEANVPFF-----FISASSFVEL---YVG 287
Cdd:COG5635 161 LNLLERIESLKRLELLEAKKKRLLILGEP-GSGKTtllrylaleLAERYLDAEDPIPILielrdLAEEASLEDLlaeALE 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 288 LGAKRVREMFKEARKLAPAIIFIDELDAVGRSrgsgigggnDEREQTLNQILVEMDGINENAGILimgaTNRTDVLDPAL 367
Cdd:COG5635 240 KRGGEPEDALERLLRNGRLLLLLDGLDEVPDE---------ADRDEVLNQLRRFLERYPKARVII----TSRPEGYDSSE 306
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14090194 368 LRpgRFDRIITVGLpDIKEREEILK-----LHSKGKRLSKEIK 405
Cdd:COG5635 307 LE--GFEVLELAPL-SDEQIEEFLKkwfeaTERKAERLLEALE 346
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
238-263 2.51e-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: 41.18  E-value: 2.51e-03
                        10        20
                ....*....|....*....|....*...
gi 14090194 238 AAAGarfpkG--ILLGGPPGTGKTLLAK 263
Cdd:COG0606 207 AAAG-----GhnLLMIGPPGSGKTMLAR 229
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
248-314 3.04e-03

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


Pssm-ID: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 39.46  E-value: 3.04e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPFFFIS---ASSFVEL------YVGLGAKRVREMFKEARKLAPaIIFIDELD 314
Cdd:cd19500  40 LCLVGPPGVGKTSLGKSIARALGRKFVRISlggVRDEAEIrghrrtYVGAMPGRIIQALKKAGTNNP-VFLLDEID 114
44 PHA02544
clamp loader, small subunit; Provisional
243-280 3.28e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 40.36  E-value: 3.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 14090194  243 RFPKGILLGGPPGTGKTLLAKATAGEANVPFFFISASS 280
Cdd:PHA02544  41 RIPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNGSD 78
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
248-313 3.86e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 39.38  E-value: 3.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194  248 ILLGGPPGTGKTLLAKAT---AGEANVPFFFISASSFVELYvgLGAKRVREMFKEARKLA-PAIIFIDEL 313
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALgyaACRQGYRVRFTTAADLVEQL--AQARADGRLGRLLRRLArYDLLIIDEL 160
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
248-276 5.98e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 39.38  E-value: 5.98e-03
                        10        20
                ....*....|....*....|....*....
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPFFFI 276
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
243-313 7.06e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 39.75  E-value: 7.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14090194 243 RFPKGILLGGPPGTGKT----LLAKATAGEANVPFFFISA------SSFVE-LYVGLGAKRVR---EMFKEARKLA---- 304
Cdd:COG1401 219 KTKKNVILAGPPGTGKTylarRLAEALGGEDNGRIEFVQFhpswsyEDFLLgYRPSLDEGKYEptpGIFLRFCLKAeknp 298
                        90
                ....*....|.
gi 14090194 305 --PAIIFIDEL 313
Cdd:COG1401 299 dkPYVLIIDEI 309
PRK13341 PRK13341
AAA family ATPase;
249-312 7.44e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.65  E-value: 7.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14090194  249 LLGGPPGTGKTLLAKATAGEANVPFFFISAssfvelyVGLGAKRVREMFKEAR--------KLapaIIFIDE 312
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA-------VLAGVKDLRAEVDRAKerlerhgkRT---ILFIDE 117
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
248-313 7.89e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 38.58  E-value: 7.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14090194   248 ILLGGPPGTGKTLLAKATAGEA---NVPFFFISASSFVELYvglgaKRVREMFKEARKLA----PAIIFIDEL 313
Cdd:pfam01695  95 VVLLGPPGVGKTHLAIALGVEAcraGYSVRFTSAADLVNQL-----KRAHGDGKLTRKLQqllkPDVLILDEW 162
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
248-273 8.02e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 39.26  E-value: 8.02e-03
                        10        20
                ....*....|....*....|....*.
gi 14090194 248 ILLGGPPGTGKTLLAKATAGEANVPF 273
Cdd:COG1219 112 ILLIGPTGSGKTLLAQTLARILDVPF 137
 
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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